Show legend Show as text

Structure type: homopolymer
Trivial name: alginate, mannuronan
Compound class: EPS, polysaccharide

• Article ID: 233
  Fett WF, Wells JM, Cescutti P, Wijey C "Identification of exopolysaccharides produced by fluorescent pseudomonads associated with commercial mushroom (Agaricus bisporus) production" - Applied and Environmental Microbiology 61 (1995) 513-517
  

  The acidic exopolysaccharides (EPSs) from 63 strains of mushroom production-associated fluorescent pseudomonads which were mucoid on Pseudomonas agar F medium (PAF) were isolated, partially purified, and characterized. The strains were originally isolated from discolored lesion which developed postharvest on mushroom (Agaricus bisporus) caps or from commercial lots of mushroom casing medium. An acidic galactoglucan, previously named marginalan, was produced by mucoid strains of the saprophyte Pseudomonas putida and the majority of mucoid strains of saprophytic P. fluorescens (biovars III and V) isolated from casing medium. One biovar II strain (J1) of P. fluorescens produced alginate, a copolymer of mannuronic and guluronic acids, and one strain (H13) produced an apparently unique EPS containing neutral and amino sugars. Of 10 strains of the pathogen "P. gingeri," the causal agent of mushroom ginger blotch, 8 gave mucoid growth on PAF. The "P. gingeri" EPS also was unique in containing both neutral sugar and glucuronic acid. Mucoid, weakly virulent strains of "P. reactans" produced either alginate or marginalan. All 10 strains of the pathogen P. tolaasii, the causal agent of brown blotch of mushrooms were nonnmucoid on PAF. Production of EPS by these 10 strains plus the 2 nonmucoid strains of "P. gingeri" also was negative on several additional solid media as well as in two broth media tested. The results support our previous studies indicating that fluorescent pseudomonads are a rich source of novel EPSs.

  Pseudomonas, exopolysaccharide, exopolysaccharides, identification, production, fluorescent, mushroom

  NCBI PubMed ID: 7574589
  Journal NLM ID: 7605801
  Publisher: American Society for Microbiology
  Institutions: Eastern Regional Research Center, U.S. Department of Agriculture, Philadelphia, Pennsulvania 19118, USA, Departement of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Trieste, Italy
  
   
  
  Pseudomonas fluorescens, Pseudomonas putida
  CSDB ID 6902 (all data & tools)
• Article ID: 391
  Svanem BIG, Strand WI, Ertesvag H, Skjak-Braek G, Hartmann M, Barbeyron T, Valla S "The catalytic activities of the bifunctional Azotobacter vinelandii mannuronan C-5-epimerase and alginate lyase AlgE7 probably originate from the same active site in the enzyme" - Journal of Biological Chemistry 276(34) (2002) 31542-31550
  

  The Azotobacter vinelandii genome encodes a family of seven secreted Ca2+-dependent epimerases (AlgE1-7) catalyzing the polymer level epimerization of b-D-mannuronic acid (M) to a-L-guluronic acid (G) in the commercially important polysaccharide alginate. AlgE1-7 are composed of two types of protein modules, A and R, and the A-modules have previously been found to be sufficient for epimerization. AlgE7 is both an epimerase and an alginase, and here we show that the lyase activity is Ca2+-dependent and also responds similarly to the epimerases in the presence of other divalent cations. The AlgE7 lyase degraded M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved were mainly G2MM and/or G2GM. Since G-moieties dominated at the reducing ends even when mannuronan was used as substrate, the AlgE7 epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities. A truncated form of AlgE1 (AlgE1-1) was converted to a combined epimerase and lyase by replacing the 5'-798 base pairs in the algE1-1 gene with the corresponding A-module-encoding DNA sequence from algE7. Furthermore, substitution of an aspartic acid residue at position 152 with glycine in AlgE7A eliminated almost all of both the lyase and epimerase activities. Epimerization and lyase activity are believed to be mechanistically related, and the results reported here strongly support this hypothesis by suggesting that the same enzymatic site can catalyze both reactions.

  activity, enzyme, site, lyase, alginate, alginate lyase, active, Azotobacter, Azotobacter vinelandii

  NCBI PubMed ID: 11390391
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: svein.valla@chembio.ntnu.no
  Institutions: From the Department of Biotechnology, Norwegian University of Science and Technology, N-7491 Trondheim, Norway, Centre d'Etudes d'Oceanologie et de Biologie Marine, CNRS, F-29680 Roscoff, France
  Methods: NMR, genetic methods
  
   
  
  Azotobacter vinelandii
  CSDB ID 8354 (all data & tools)
• Article ID: 839
  Jain S, Franklin MJ, Ertesvag H, Valla S, Ohman DE "The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa" - Molecular Microbiology 47(4) (2003) 1123-1133
  

  Pseudomonas aeruginosa strains causing chronic pulmonary infections in cystic fibrosis patients produce high levels of alginate, an exopolysaccharide that confers a mucoid phenotype. Alginate is a linear polymer of d-mannuronate (M) and variable amounts of its C-5-epimer, l-guluronate (G). AlgG is a periplasmic C-5-epimerase that converts poly d-mannuronate to the mixed M+G sequence of alginate. To understand better the role and mechanism of AlgG activity, a mutant was constructed in the mucoid strain FRD1 with a defined non-polar deletion of algG. Instead of producing poly mannuronate, the algG deletion mutant secreted dialysable uronic acids, as does a mutant lacking the periplasmic protein AlgK. High levels of unsaturated ends and the nuclear magnetic resonance spectroscopy pattern revealed that the small, secreted uronic acids were the products of extensive polymer digestion by AlgL, a periplasmic alginate lyase co-expressed with AlgG and AlgK. Thus, AlgG is bifunctional with (i) epimerase activity and (ii) a role in protecting alginate from degradation by AlgL during transport through the periplasm. AlgK appears to share the second role. AlgG and AlgK may be part of a periplasmic protein complex, or scaffold, that guides alginate polymers to the outer membrane secretin (AlgE). To characterize the epimerase activity of AlgG further, the algG4 allele of poly mannuronate-producing FRD462 was shown to encode a protein lacking only the epimerase function. The sequence of algG4 has a Ser-272 to Asn substitution in a serine-threonine-rich and conserved region of AlgG, which revealed a critical residue for C-5-epimerase activity

  Pseudomonas aeruginosa, exopolysaccharide, epimerase, cystic fibrosis, alginate, alginate lyase, uronic acids

  NCBI PubMed ID: 12581364
  Publication DOI: 10.1046/j.1365-2958.2003.03361.x
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: deohman@hsc.vcu.edu
  Institutions: Department of Microbiology, Medical College of Virginia Campus of Virginia Commonwealth University, 1101 E. Marshall St., Rm. 5-051, Richmond, VA 23298-0678, USA, Department of Microbiology, Medical College of Virginia Campus of Virginia Commonwealth University, Richmond, USA
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 2482 (all data & tools)
• Article ID: 2205
  Steginsky CA, Beale JM, Floss HG, Mayer RM "Structural determination of alginic acid and the effects of calcium binding as determined by high-field NMR" - Carbohydrate Research 225 (1992) 11-26
  

  The nature of the solution conformations of the alginic acid components D-mannuronan (poly-ManA) and L-guluronan (poly-GulA) from Azotobacter vinelandii were investigated by both one- and two-dimensional n.m.r. methods. Unequivocal proton assignments for both polymers as well as their constituent monomer units were made based on chemical-shift theory, coupling constant analysis, and nuclear Overhauser enhancement measurements. These data were used to investigate the interactions of poly-GulA and poly-ManA with Ca2+ ion in aqueous medium. Based on relative crosspeak integrals measured in two-dimensional phase-sensitive NOESY spectra of free and calcium-bound polymer, a model for calcium binding is proposed.

  NCBI PubMed ID: 1633597
  Publication DOI: 10.1016/0008-6215(92)80036-z
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Chemistry, Ohio State University, Columbus 43210
  Methods: 1H NMR, NMR-2D
  
   
  
  Azotobacter vinelandii
  CSDB ID 116488 (all data & tools)
• Article ID: 2751
  Sutherland IW "Industrially useful microbial polysaccharides" - Microbiological Sciences 3 (1986) 5-9
  

  A number of microbial exopolysaccharides possess properties of industrial importance, especially as viscosifiers and gelling agents. This group of biopolymers is diverse in its chemical composition and structure; it includes both anionic and neutral polysaccharides, most of which are of bacterial origin.

  mannuronan

  NCBI PubMed ID: 3153140
  Journal NLM ID: 8510101
  Institutions: Department of Microbiology, Edinburgh University, UK
  
   
  
  Azotobacter vinelandii, Pseudomonas aeruginosa
  CSDB ID 143640 (all data & tools)
• Article ID: 2898
  Pecina A, Paneque A "Studies on some enzymes of alginic acid biosynthesis in mucoid and nonmucoid Azotobacter chroococcum strains" - Applied Biochemistry and Biotechnology 49 (1994) 51-58
  
  Journal NLM ID: 8208561
  Publisher: Humana Press
  
   
  
  Azotobacter chroococcum ATCC 4412
  CSDB ID 103983 (all data & tools)
• Article ID: 2990
  Espevik T, Otterlei M, Skjak-Braek G, Ryan L, Wright SD, Sundan A "The involvement of CD14 in stimulation of cytokine producion by uronic acid polymers" - European Journal of Immunology 23 (1993) 255-261
  
  Journal NLM ID: 1273201
  
   
  
  Pseudomonas syringae pv. phaseolicola
  CSDB ID 124994 (all data & tools)
• Article ID: 3228
  Jerga A, Stanley MD, Tipton PA "Chemical mechanism and specificity of the C5-mannuronan epimerase reaction" - Biochemistry 45(30) (2006) 9138-9144
  

  C5-mannuronan epimerase catalyzes the formation of α-L-guluronate residues from β-D-mannuronate residues in the synthesis of the linear polysaccharide alginate. The reaction requires the abstraction of a proton from C5 of the residue undergoing epimerization followed by re-protonation on the opposite face. Rapid-mixing chemical quench experiments were conducted to determine the nature of the intermediate formed upon proton abstraction in the reaction catalyzed by the enzyme from Pseudomonas aeruginosa. Colorimetric and HPLC analysis of quenched samples indicated that shortened oligosaccharides containing an unsaturated sugar residue form as transient intermediates in the epimerization reaction. This suggests that the carbanion is stabilized by glycal formation, concomitant with cleavage of the glycosidic bond between the residue undergoing epimerization and the adjacent residue. The time dependence of glycal formation suggested that slow steps flank the chemical steps in the catalytic cycle. Solvent isotope effects on V and V/K were unity, consistent with a catalytic cycle in which chemistry is not rate-limiting. The specificity of the epimerase with regard to neighboring residues was examined, and it was determined that the enzyme showed no bias for mannuronate residues adjacent to guluronates versus those adjacent to mannuronates. Proton abstraction and sugar epimerization were irreversible. Existing guluronate residues already present in the polysaccharide were not converted to mannuronates, nor was incorporation of solvent deuterium into existing mannuronates observed.

  Pseudomonas aeruginosa, specificity, mechanism, alginate, C5-mannuronan epimerase

  NCBI PubMed ID: 16866359
  Publication DOI: 10.1021/bi060748f
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Correspondence: tiptonp@missouri.edu
  Institutions: Department of Biochemistry, University of Missouri, Columbia, MO, USA
  Methods: NMR, biochemical methods
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 20033 (all data & tools)
• Article ID: 3627
  Otterlei M, Sundan A, Skjak-Braek G, Ryan L, Smidsrod O, Espevik T "Similar mechanism of action of defined polysaccharides and lipopolysaccharides: characterization of binding and tumor necrosis factor alpha induction" - Infection and Immunity 61(5) (1993) 1917-1925
  

  Little has been reported about the effects of different polysaccharides on cytokine production from human monocytes. In this study, we show that several well-defined polysaccharides, including polymers with different sizes of β 1-4-linked D-mannuronic acid (poly-M, high-M alginate, and M-blocks) and cellulose oxidized in the C-6 position, induced human monocytes to produce tumor necrosis factor alpha (TNF-α). Poly-M was the most efficient polysaccharide tested and, on a weight basis, was approximately as efficient as lipopolysaccharide (LPS) from Escherichia coli. TNF-α production was shown to depend strongly on the molecular weights of poly-M and high-M alginate, with maximal TNF-α production occurring at molecular weights above 50,000 and 200,000, respectively. G-blocks, α1-4-linked L-guluronic acid polymers that did not induce cytokine production from monocytes, reduced the cytokine production induced by the β 1-4-linked polyuronic acids and LPS. Furthermore, both G-blocks and LPS were found to inhibit the binding of poly-M to monocytes, as measured by flow cytometry. In addition, we found that the binding of LPS to monocytes was inhibited by G-blocks, M-blocks, and poly-M. Our results indicate that β 1-4-linked polyuronic acids and LPS may stimulate monocytes to produce TNF-α by similar mechanisms and may bind to a common receptor.

  binding, alginate, tumor necrosis factor, cytokine, Monocytes

  NCBI PubMed ID: 8478081
  Publication DOI: 10.1128/IAI.61.5.1917-1925.1993
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Institute of Cancer Research, University of Trondheim, Norway.
  Methods: cytokines tumor necrosis factor alpha (TNF-a) assay, interleukin-1 assay
  
   
  
  Pseudomonas aeruginosa O5
  CSDB ID 24821 (all data & tools)
• Article ID: 4287
  Cote GL, Krull LH "Characterization of the exocellular polysaccharides from Azotobacter chroococcum" - Carbohydrate Research 181 (1988) 143-152
  

  Azotobacter chroococcum produces appreciable amounts of exocellular polysaccharide. Produced by A. chroococcum strain NRRL B-14341 are at least two distinct polysaccharides which can be separated by ion-exchange chromatography on DEAE-Sephadex A-25. Exopolysaccharide I (EPS-I) consists of rhamnose, mannose, and galactose in the molar ratios of 1:2:2, along with a trace of glucose. EPS-I also contains pyruvic acetal and acetic ester groups. Exopolysaccharide II (EPS-II) consists mainly of mannuronic acid, with much smaller proportions of guluronic acid. Acetic ester groups are also present in EPS-II. Methylation analysis of reduced EPS-II shows it to be (1→4)-linked, and 13C-nuclear magnetic resonance spectroscopy indicates that it is mainly (1→4)-β-d-mannuronan. EPS-II is evidently a low-guluronate form of alginate. Batch-to-batch variation was observed in the relative amounts of the two polysaccharides, the acetyl and pyruvic contents of EPS-I, and the degree of acetylation of EPS-II.

  structure, exopolysaccharide, Azotobacter chroococcum

  Publication DOI: 10.1016/0008-6215(88)84030-8
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Northern Regional Research Center, Agricultural Research Service, United States Department of Agriculture, 1815 North University Street, Peoria, IL 61604 U.S.A.
  Methods: 13C NMR, 1H NMR, methylation, GLC-MS, sugar analysis, GLC, HPAEC, GC, GPC
  
   
  
  Azotobacter chroococcum NRRL B-14341
  CSDB ID 27138 (all data & tools)
• Article ID: 12516
  Nagaoka M, Shibata H, Kimura-Takagi I, Hashimoto S, Aiyama R, Ueyama S, Yokokura T "Anti-ulcer effects and biological activities of polysaccharides from marine algae" - BioFactors 12(1-4) (2000) 267-274
  

  The nutritional value of marine algae has long been recognized in the Orient, but in the Western world, the use of seaweeds for human consumption is limited: they exist as additives and so-called health foods. In contrast, more seaweed than ever before is being eaten in Japan, China and Korea. Seaweeds are low in fats, and contain vitamins and minerals [1,2]. They also contain a large quantity of chemically characteristic mucilaginous polysaccharides such as agar, carrageenans, alginate, laminaran, rhamnan sulfate and fucoidan. These polysaccharides differ from those in terrestrial vegetables and provide dietary fiber: the human body does not digest them [3]. These polysaccharides are used in the food and pharmaceutical industries and have recently been demonstrated to have some unique biological activities. In this paper, we review the structure and function of marine algal polysaccharides, especially the anti-ulcer effect of fucoidan.

  polysaccharides, algae, anti-ulcer effects, seaweeds, fucoidan

  NCBI PubMed ID: 11216495
  Publication DOI: 10.1002/biof.5520120140
  Journal NLM ID: 8807441
  Publisher: Oxford; Washington, DC: IRL Press, International Union of Biochemistry
  Correspondence: masato-nagaoka@yakult.co.jp
  Institutions: Yakult Central Institute for Microbiological Research, Kunritachi, Japan
  
   
  
  (Phaeophyceae)
  CSDB ID 67022 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: alginate, alginate oligosaccharide, alginic acid
Compound class: EPS

• Article ID: 233
  Fett WF, Wells JM, Cescutti P, Wijey C "Identification of exopolysaccharides produced by fluorescent pseudomonads associated with commercial mushroom (Agaricus bisporus) production" - Applied and Environmental Microbiology 61 (1995) 513-517
  

  The acidic exopolysaccharides (EPSs) from 63 strains of mushroom production-associated fluorescent pseudomonads which were mucoid on Pseudomonas agar F medium (PAF) were isolated, partially purified, and characterized. The strains were originally isolated from discolored lesion which developed postharvest on mushroom (Agaricus bisporus) caps or from commercial lots of mushroom casing medium. An acidic galactoglucan, previously named marginalan, was produced by mucoid strains of the saprophyte Pseudomonas putida and the majority of mucoid strains of saprophytic P. fluorescens (biovars III and V) isolated from casing medium. One biovar II strain (J1) of P. fluorescens produced alginate, a copolymer of mannuronic and guluronic acids, and one strain (H13) produced an apparently unique EPS containing neutral and amino sugars. Of 10 strains of the pathogen "P. gingeri," the causal agent of mushroom ginger blotch, 8 gave mucoid growth on PAF. The "P. gingeri" EPS also was unique in containing both neutral sugar and glucuronic acid. Mucoid, weakly virulent strains of "P. reactans" produced either alginate or marginalan. All 10 strains of the pathogen P. tolaasii, the causal agent of brown blotch of mushrooms were nonnmucoid on PAF. Production of EPS by these 10 strains plus the 2 nonmucoid strains of "P. gingeri" also was negative on several additional solid media as well as in two broth media tested. The results support our previous studies indicating that fluorescent pseudomonads are a rich source of novel EPSs.

  Pseudomonas, exopolysaccharide, exopolysaccharides, identification, production, fluorescent, mushroom

  NCBI PubMed ID: 7574589
  Journal NLM ID: 7605801
  Publisher: American Society for Microbiology
  Institutions: Eastern Regional Research Center, U.S. Department of Agriculture, Philadelphia, Pennsulvania 19118, USA, Departement of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Trieste, Italy
  
   
  
  Pseudomonas fluorescens, Pseudomonas putida
  CSDB ID 6904 (all data & tools)
• Article ID: 350
  Pier GB "Rationale for development of immunotherapies that target mucoid Pseudomonas aeruginosa infection in cystic fibrosis patient" - Behring Institute Mitteilungen 98 (1997) 350-360
  

  Despite a complex sputum bacteriology, the progressive decline in pulmonary function that is the hallmark of the genetic disease cystic fibrosis (CF) is attributable to a single infecting pathogen, mucoid Pseudomonas aeruginosa. Therefore, active and passive immunotherapies that target this particular variant of the bacterium should be of value in attenuating infection and interfering with the decline in pulmonary function. The major surface antigen of mucoid P. aeruginosa is raferred to as either mucoid exopolysaccharide (MEP) or alginate, a random polymer of D-mannuronic and L-guluronic acid residues linked b 1-4. During chronic infection CF patients make antibodies to MEP that fail to mediate opsonic killing of bacteria in vitro. Thewe antibodies can be elicited by vaccination in 35-40% of plasma donors given a preparation of MEP comprised of only the bighest molecular-weight polymers; inclusion in human vaccines of smaller polymers normally produced by the bacterium fails to elicit opsonic antibodies, just like in infected CF pationts. Opsonic, byt not non-opsonic, antibodies to MEP protect animals against chronic endobronchial infection. CF patients do produce opsonic antibodies to mucoid P. aeruginosa that are in a planktomic or suspended state, byt thewe antibodies are not directed at the MEP antigen and they fail to kill P. aeruginosa growing in a biofilm. This is the state that the bacteria grow in the lung. Therefore immunoglobulin G preparations with opsonic antibodies to MEP could provide CF patients with antibodies that they normally do not produce during chronic laung infection and may improve their clinical course.

  vaccine, mucoid P. aeruginosa, mucoid exopolysaccharide, serotherapy, cystic fibrosis

  NCBI PubMed ID: 9382760
  Journal NLM ID: 0367532
  Publisher: Marburg/Lahn: Behringwerke AG
  Institutions: Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115 5899, USA
  Methods: biological assays
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 8012 (all data & tools)
• Article ID: 351
  Pier GB, Coleman F, Grout M, Franklin M, Ohman DE "Role of alginate O acetylation in resistance of mucoid Pseudomonas aeruginosa to opsonic phagocytosis" - Infection and Immunity 69(3) (2001) 1895-1901
  

  Establishment and maintenance of chronic lung infections with mucoid Pseudomonas aeruginosa in patients with cystic fibrosis (CF) require that the bacteria avoid host defenses. Elaboration of the extracellular, O-acetylated mucoid exopolysaccharide, or alginate, is a major microbial factor in resistance to immune effectors. Here we show that O acetylation of alginate maximizes the resistance of mucoid P. aeruginosa to antibody-independent opsonic killing and is the molecular basis for the resistance of mucoid P. aeruginosa to normally nonopsonic but alginate-specific antibodies found in normal human sera and sera of infected CF patients. O acetylation of alginate appears to be critical for P. aeruginosa resistance to host immune effectors in CF patients.

  Pseudomonas, O-acetylation, resistance, phagocytosis, acetylation, alginate, mucoid Pseudomonas aeruginosa, opsonic

  NCBI PubMed ID: 11179370
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: gpier@channing.harvard.edu
  Institutions: Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115-58041, Department of Microbiology, Montana State University, Bozeman, Montana 597172, Department of Microbiology and Immunology, Medical College of Virginia Campus of Virginia Commonwealth University, Richmond, Virginia 23298-06783, McGuire Veterans Affairs Medical Center, Richmond, Virginia 232494
  Methods: biological assays
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 8013 (all data & tools)
• Article ID: 365
  Russo A, Moënne-Loccoz Y, Fedi S, Higgins P, Fenton A, Dowling DN, O'Regan M, O'Gara F "Improved delivery of biocontrol Pseudomonas and their antifungal metabolites using alginate polymers" - Applied Microbiology and Biotechnology 44 (1996) 740-745
  

  Alginate polymer was evaluated as a carrier for seed inoculation with a genetically modified strain Pseudomonas fluorescens F113LacZY, which protects sugar-beet against Pythium-mediated damping-off. F113LacZY survived in alginate beads at 5 log10 CFU/bead or higher counts for 8 weeks of storage, regardless of the conditions of incubation. In plant inoculation experiments, colonisation of the growing area of the root by F113LacZY, derived from alginate beads placed in the soil next to the seed or from an alginate coating around the seeds, was improved compared with application of just free cells of the strain. F113LacZY trapped in alginate beads was an effective producer of antifungal phloroglucinols as indicated by direct HPLC quantification of phloroglucinols and in vitro inhibition of both the indicator bacterium Bacillus subtilis A1 and the pathogenic fungus Pythium ultimum. Alginate polymer represents a promising carrier for the delivery of biocontrol inoculants for root colonisation and production of antifungal metabolites.

  Pseudomonas, polymer, alginate, metabolite, Polymers

  NCBI PubMed ID: 8867631
  Journal NLM ID: 8406612
  Publisher: Springer
  Institutions: Microbiology Department, University College Cork, Cork, Ireland
  Methods: biological assays
  
   
  
  Pseudomonas fluorescens
  CSDB ID 8069 (all data & tools)
• Article ID: 368
  Sawabe T, Takahashi H, Ezura Y, Gacesa P "Cloning, sequence analysis and expression of Pseudoalteromonas elyakovii IAM 14594 gene (alyPEEC) encoding the extracellular alginate lyase" - Carbohydrate Research 335(1) (2001) 11-21
  

  A gene (alyPEEC) encoding an alginate lyase of Pseudoalteromonas elyakovii IAM 14594 was cloned using the plasmid vector pUC118 and expressed in Escherichia coli. Sequencing of a 3.0kb fragment revealed a 1,197bp open reading frame encoding 398 amino acid residues. The calculated molecular mass and isoelectric point of the alyPEEC gene product are 43.2 kDa and pI 5.29. A region G(165) to V(194) in the AlyPEEC internal sequence is identical to the N-terminal amino acid sequence of the previously purified extracellular alginate lyase of P. elyakovii, and the calculated molecular mass (25.4 kDa) and isoelectric point (pI 4.78) of the region resembled those of the purified enzyme. Expression of enzymically-active alginate lyase from alyPEEC required growth of recombinant E. coli in LB broth containing 50% (v/v) artificial seawater (ASW). Alginate lyase activity with broad substrate specificity was detected in both 42 and 30 kDa products. Subcloning of the region G(165) to N(398) of AlyPEEC corresponding to the 30 kDa protein confirmed that this region of the alyPEEC gene encoded the active site of the enzyme. A region A(32) to G(164) corresponding to about 13 kDa of the N-terminal region of AlyPEEC showed about 30% identity to a putative chitin binding domain of Streptomyces chitinases, but did not exhibit any catalytic activity.

  Sequence Analysis, cloning, alginate lyase, bacterial enzymes, Pseudoalteromonas elyakovii

  NCBI PubMed ID: 11553350
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: sawabe@pop.fish.hokudai.ac.jp
  Institutions: Laboratory of Microbiology, Graduate School of Fisheries Sciences, Hokkaido University, 3-1-1 Minato-cho, Hakodate 041-8611, Japan
  Methods: genetic methods
  
   
  
  Pseudoalteromonas elyakovii IAM 14594
  CSDB ID 8079 (all data & tools)
• Article ID: 510
  Zhang Z, Yu G, Guan H, Zhao X, Du Y, Jiang X "Preparation and structure elucidation of alginate oligosaccharides degraded by alginate lyase from Vibro sp. 510" - Carbohydrate Research 339(8) (2004) 1475-1481
  

  Alginate that was purified from the fermentation solution of marine bacteria Vibro sp. 510 under specific reaction conditions was hydrolyzed by alginate lyase. Seven oligosaccharides, including di-, tri- and tetrasaccharides, were isolated through low-pressure, gel-permeation chromatography (LP-GPC) and semipreparative strong-anion exchange (SAX) fast-protein liquid chromatography (FPLC). The oligosaccharide structures were elucidated based on ESIMS and 2D NMR spectral analysis. The hydrolytic specificity of this alginate lyase to alginate is discussed.

  Oligosaccharides, alginate, alginate lyase, guluronic acid, mannuronic acid

  NCBI PubMed ID: 15178390
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: glyu@mail.ouc.edu.cn
  Institutions: Institute of Marine Drug and Food, Ocean University of China, Qingdao, China, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China, Department of Food Science and Technology, Ocean University of China, Qingdao, China
  Methods: gel filtration, NMR-2D, enzymatic hydrolysis, ESI-MS, anion-exchange chromatography, fast protein chromatography
  
   
  
  (bacteria)
  CSDB ID 9241 (all data & tools)
• Article ID: 744
  Kidambi SP, Sundin GW, Palmer DA, Chakrabarty AM, Bender CL "Copper as a signal for alginate synthesis in Pseudomonas syringae pv. syringae" - Applied and Environmental Microbiology 61 (1995) 2172-2179
  

  Plant-associated pseudomonads are commonly exposed to copper bactericides, which are applied to reduce the disease incidence caused by these bacteria. Consequently, many of these bacteria have acquired resistance or tolerance to copper salts. We recently conducted a survey of 37 copper-resistant (Cur) Pseudomonas spp., including P. cepacia, P. fluorescens, P. syringae, and P. viridiflava, and found that a subset of the P. syringae strains showed a dramatic increase in exopolysaccharide (EPS) production on mannitol-glutamate medium containing CuSO4 at 250 micrograms/ml. A modified carbazole assay indicated that the EPS produced on copper-amended media contained high levels of uronic acids, suggesting that the EPS was primarily alginic acid. Uronic acids extracted from selected strains were further confirmed to be alginate by demonstrating their sensitivity to alginate lyase and by descending paper chromatography following acid hydrolysis. Subinhibitory levels of arsenate, cobalt, lithium, rubidium, molybdenum, and mercury did not induce EPS production, indicating that alginate biosynthesis is not induced in P. syringae cells exposed to these heavy metals. A 200-kb plasmid designated pPSR12 conferred a stably mucoid phenotype to several P. syringae recipients and also increased their resistance to cobalt and arsenate. A cosmid clone constructed from pPSR12 which conferred a stably mucoid phenotype to several P. syringae strains but not to Pseudomonas aeruginosa was obtained. Results obtained in this study indicate that some of the signals and regulatory genes for alginate production in P. syringae differ from those described for alginate production in P. aeruginosa.

  synthesis, Pseudomonas, signal, Pseudomonas syringae, alginate, copper

  NCBI PubMed ID: 7793938
  Journal NLM ID: 7605801
  Publisher: American Society for Microbiology
  Institutions: Department of Plant Pathlogy, Oklahoma State University, Stillwater, USA
  
   
  
  Pseudomonas syringae pv. syringae
  CSDB ID 881 (all data & tools)
• Article ID: 1003
  Monday SR, Schiller NL "Alginate synthesis in Pseudomonas aeruginosa: The role of AlgL (alginate lyase) and AlgX" - Journal of Bacteriology 178 (1996) 625-632
  

  synthesis, role, Pseudomonas, Pseudomonas aeruginosa, lyase, alginate, alginate lyase

  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: Neals@ucracl.ucr.edu
  Institutions: Division of Biomedical Sciences, University of California, Riverside, CA, USA
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 3471 (all data & tools)
• Article ID: 1012
  Morea A, Mathee K, Franklin MJ, Giacomini A, O'Regan M, Ohman DE "Characterization of algG encoding C5-epimerase in the alginate biosynthetic gene cluster of Pseudomonas fluorescens" - Gene 278(1-2) (2001) 107-114
  

  The organization of the alginate gene cluster in Pseudomonas fluorescens was characterized. A bank of genomic DNA from P. fluorescens was mobilized to a strain of Pseudomonas aeruginosa with a transposon insertion (algJ::Tn501) in the alginate biosynthetic operon that rendered it non-mucoid. Phenotypic complementation in this heterologous host was observed, and a complementing clone containing 32 kb of P. fluorescens DNA was obtained. Southern hybridization studies showed that genes involved in alginate biosynthesis (e.g. algD, algG, and algA) were approximately in the same order and position as in P. aeruginosa. When the clone was mobilized to a P. aeruginosa algG mutant that produced alginate as polymannuronate due to its C5-epimerase defect, complementation was observed and the alginate from the recombinant strain contained L-guluronate as determined by proton nuclear magnetic resonance spectroscopy. A sequence analysis of the P. fluorescens DNA containing algG revealed sequences similar to P. aeruginosa algG that were also flanked by algE- and algX-like sequences. The predicted AlgG amino acid sequence of P. fluorescens was 67% identical (80% similar) to P. aeruginosa AlgG and 60% identical (76% similar) to Azotobacter vinelandii AlgG. As in P. aeruginosa, AlgG from P. fluorescens appeared to have a signal sequence that would localize it to the periplasm where AlgG presumably acts as a C5- epimerase at the polymer level. Non-polar algG knockout mutants of P. fluorescens were defective in alginate production, suggesting a potential role for this protein in polymer formation

  biosynthesis, complementation, biosynthetic, chemistry, gene, Bacterial, genetics, growth & development, host, metabolism, phenotype, potential, role, Sequence Analysis, DNA, strain, Support, characterization, polysaccharide, analysis, Pseudomonas, Pseudomonas aeruginosa, molecular, polymer, acid, cloning, level, Molecular Sequence Data, protein, signal, cluster, gene cluster, Multigene Family, mutant, mutants, epimerase, insertion, position, production, transposon, Magnetic Resonance Spectroscopy, nuclear, nuclear magnetic resonance, nuclear magnetic resonance spectroscopy, resonance, spectroscopy, sequence, mutation, formation, Pseudomonas fluorescens, amino, clone, biotechnology, Base Sequence, heterologous, mutagenesis, operon, amino acid, recombinant, organization, alginate, Azotobacter, Azotobacter vinelandii, U.S.Gov't, Non-P.H.S., order, amino acid sequence, Sequence Alignment, Sequence Homology, P.H.S., Carbohydrate Epimerases, alga, alginate biosynthesis, alginate gene, alginate production, Alginates, Cell Division, Gene Order, Insertional, nonmucoid, periplasm, phenotypic, proton, capsula, heterologuos complementation

  NCBI PubMed ID: 11707327
  Journal NLM ID: 7706761
  Publisher: Amsterdam: Elsevier
  Institutions: CRIBI, Biotechnology Centre, University of Padova, Viale G. Colombo 3, 35121 Padova, Italy
  
   
  
  Pseudomonas fluorescens
  CSDB ID 3500 (all data & tools)
• Article ID: 1370
  Beale JM, Foster JL "Carbohydrate fluxes into alginate biosynthesis in Azotobacter vinelandii NCIB 8789: NMR investigations of the triose pools" - Biochemistry 35(14) (1996) 4492-4501
  

  NMR, biosynthesis, carbohydrate, alginate, Azotobacter, Azotobacter vinelandii, alginate biosynthesis

  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Institutions: Division of Medicinal and Natural Products Chemistry, College of Pharmacy,USA
  Methods: NMR
  
   
  
  Azotobacter vinelandii NCIB8789
  CSDB ID 6249 (all data & tools)
• Article ID: 1376
  Blatny JM, Ertesvag H, Nes IF, Valla S "Heterologous gene expression in Lactococcus lactis; expression of the Azotobacter vinelandii algE6 gene product displaying mannuronan C-5 epimerase activity" - FEMS Microbiology Letters 227(2) (2003) 229-235
  

  The Azotobacter vinelandii mannuronan C-5 epimerases AlgE1-7 can be used to improve the properties of the commercially important polysaccharide alginate that is widely used in a variety of products, such as food and pharmaceuticals. Since lactic acid bacteria are generally regarded as safe, they are attractive candidates for production of the epimerases. A. vinelandii genes are GC-rich, in contrast to those of lactic acid bacteria, but we show here that significant expression levels of the epimerase AlgE6 can be obtained in Lactococcus lactis using the nisin-controlled expression system. A 1200-fold induction ratio was obtained resulting in an epimerase activity of 23900 dpm mg(-1) h(-1), using a tritiated alginate substrate. The epimerase was detected by Western blotting and nuclear magnetic resonance spectroscopy analysis of its reaction product showed that the enzyme displayed catalytic properties similar to those produced in Escherichia coli

  blotting, chemistry, expression, gene, polysaccharide, analysis, food, property, Escherichia, Escherichia coli, acid, level, Lactic acid bacteria, bacteria, activity, epimerase, production, Magnetic Resonance Spectroscopy, nuclear, nuclear magnetic resonance, nuclear magnetic resonance spectroscopy, resonance, spectroscopy, Lactococcus lactis, enzyme, Lactococcus, biotechnology, gene expression, heterologous, lactic acid bacterium, reaction, substrate, alginate, Azotobacter, Azotobacter vinelandii, pharmaceutical, induction, lactic acid

  NCBI PubMed ID: 14592713
  Journal NLM ID: 7705721
  Publisher: Blackwell Publishing
  Correspondence: janet.blatny@ikb.nlh.no
  Institutions: Laboratory of Microbial Gene Technology, Department of Chemistry and Biotechnology, Agricultural University of Norway, P.O. Box 5051, N-1432, As, Norway
  
   
  
  Lactococcus lactis, Azotobacter vinelandii
  CSDB ID 6266 (all data & tools)
• Article ID: 1404
  Clementi F, Fantozzi P, Mancini F, Moresi M "Optimal conditions for alginate production by Azotobacter vinelandii" - Enzyme and Microbial Technology 17 (1995) 983-988
  

  polysaccharide, bacteria, production, alginate, Azotobacter, Azotobacter vinelandii, alginate production, experimental design, optimization

  Journal NLM ID: 8003761
  Institutions: Instituto di Industrie agrarie, Universita di Perugia, Perugia, Italy
  
   
  
  Azotobacter vinelandii
  CSDB ID 6535 (all data & tools)
• Article ID: 1621
  Jain S, Ohman DE "Role of an alginate lyase for alginate transport in mucoid Pseudomonas aeruginosa" - Infection and Immunity 73(10) (2005) 6429-6436
  

  The opportunistic pathogen Pseudomonas aeruginosa secretes a capsule-like polysaccharide called alginate that is important for evasion of host defenses, especially during chronic pulmonary disease of patients with cystic fibrosis (CF). Most proteins for alginate biosynthesis are encoded by the 12-gene algD operon. Interestingly, this operon also encodes AlgL, a lyase that degrades alginate. Mutants lacking AlgG, AlgK, or AlgX, also encoded by the operon, synthesize alginate polymers that are digested by the coregulated protein AlgL. We examined the phenotype of an ∆algL mutation in the highly mucoid CF isolate FRD1. Generating a true ∆algL mutant was possible only when the algD operon was under the control of a LacI(q)-repressed trc promoter. Upon induction of alginate production with isopropyl-β-D-thiogalactopyranoside, the ∆algL mutant cells were lysed within a few hours. Electron micrographs of the ∆algL mutant showed that alginate polymers accumulated in the periplasm, which ultimately burst the bacterial cell wall. The requirement of AlgL in an alginate-overproducing strain led to a new model for alginate secretion in which a multiprotein secretion complex (or scaffold, that includes AlgG, AlgK, AlgX, and AlgL) guides new polymers through the periplasm for secretion across the outer membrane. In this model, AlgL is bifunctional with a structural role in the scaffold and a role in degrading free alginate polymers in the periplasm.

  role, Pseudomonas, Pseudomonas aeruginosa, lyase, alginate, mucoid Pseudomonas aeruginosa, alginate lyase, transport, mucoid

  NCBI PubMed ID: 16177314
  Publication DOI: 10.1128/IAI.73.10.6429-6436.2005
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: deohman@hsc.vcu.edu
  Institutions: Department of Microbiology and Immunology, Medical College of Virginia Campus of Virginia Commonwealth University, Richmond, 23298-0678, USA
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 10556 (all data & tools)
• Article ID: 3228
  Jerga A, Stanley MD, Tipton PA "Chemical mechanism and specificity of the C5-mannuronan epimerase reaction" - Biochemistry 45(30) (2006) 9138-9144
  

  C5-mannuronan epimerase catalyzes the formation of α-L-guluronate residues from β-D-mannuronate residues in the synthesis of the linear polysaccharide alginate. The reaction requires the abstraction of a proton from C5 of the residue undergoing epimerization followed by re-protonation on the opposite face. Rapid-mixing chemical quench experiments were conducted to determine the nature of the intermediate formed upon proton abstraction in the reaction catalyzed by the enzyme from Pseudomonas aeruginosa. Colorimetric and HPLC analysis of quenched samples indicated that shortened oligosaccharides containing an unsaturated sugar residue form as transient intermediates in the epimerization reaction. This suggests that the carbanion is stabilized by glycal formation, concomitant with cleavage of the glycosidic bond between the residue undergoing epimerization and the adjacent residue. The time dependence of glycal formation suggested that slow steps flank the chemical steps in the catalytic cycle. Solvent isotope effects on V and V/K were unity, consistent with a catalytic cycle in which chemistry is not rate-limiting. The specificity of the epimerase with regard to neighboring residues was examined, and it was determined that the enzyme showed no bias for mannuronate residues adjacent to guluronates versus those adjacent to mannuronates. Proton abstraction and sugar epimerization were irreversible. Existing guluronate residues already present in the polysaccharide were not converted to mannuronates, nor was incorporation of solvent deuterium into existing mannuronates observed.

  Pseudomonas aeruginosa, specificity, mechanism, alginate, C5-mannuronan epimerase

  NCBI PubMed ID: 16866359
  Publication DOI: 10.1021/bi060748f
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Correspondence: tiptonp@missouri.edu
  Institutions: Department of Biochemistry, University of Missouri, Columbia, MO, USA
  Methods: NMR, biochemical methods
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 20310 (all data & tools)
• Article ID: 4639
  Whitney JC, Howell PL "Synthase-dependent exopolysaccharide secretion in Gram-negative bacteria" - Trends in Microbiology 21(2) (2013) 63-72
  

  The biosynthesis and export of bacterial cell-surface polysaccharides is known to occur through several distinct mechanisms. Recent advances in the biochemistry and structural biology of several proteins in synthase-dependent polysaccharide secretion systems have identified key conserved components of this pathway in Gram-negative bacteria. These components include an inner-membrane-embedded polysaccharide synthase, a periplasmic tetratricopeptide repeat (TPR)-containing scaffold protein, and an outer-membrane beta-barrel porin. There is also increasing evidence that many synthase-dependent systems are post-translationally regulated by the bacterial second messenger bis-(3'-5')-cyclic dimeric guanosine monophosphate (c-di-GMP). Here, we compare these core proteins in the context of the alginate, cellulose, and poly-β-D-N-acetylglucosamine (PNAG) secretion systems.

  exopolysaccharide, alginate, cellulose, synthase, poly-β-D-N-acetylglucosamine

  NCBI PubMed ID: 23117123
  Publication DOI: 10.1016/j.tim.2012.10.001
  Journal NLM ID: 9310916
  Publisher: Cambridge: Elsevier Trends Journals
  Correspondence: Howell PL
  Institutions: Program in Molecular Structure and Function, The Hospital for Sick Children, 555 University Avenue, Toronto, ON M5G 1X8, Canada
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 29812 (all data & tools)
• Article ID: 5492
  Schmid J, Sieber V, Rehm B "Bacterial exopolysaccharides: biosynthesis pathways and engineering strategies" - Frontiers in Microbiology 6 (2015) 496
  

  Bacteria produce a wide range of exopolysaccharides which are synthesized via different biosynthesis pathways. The genes responsible for synthesis are often clustered within the genome of the respective production organism. A better understanding of the fundamental processes involved in exopolysaccharide biosynthesis and the regulation of these processes is critical toward genetic, metabolic and protein-engineering approaches to produce tailor-made polymers. These designer polymers will exhibit superior material properties targeting medical and industrial applications. Exploiting the natural design space for production of a variety of biopolymer will open up a range of new applications. Here, we summarize the key aspects of microbial exopolysaccharide biosynthesis and highlight the latest engineering approaches toward the production of tailor-made variants with the potential to be used as valuable renewable and high-performance products for medical and industrial applications.

  biosynthesis, gene clusters, Bacterial exopolysaccharides, polysaccharide engineering, tailor-made exopolysaccharides

  NCBI PubMed ID: 26074894
  Publication DOI: 10.3389/fmicb.2015.00496
  Journal NLM ID: 101548977
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: Jochen Schmid
  Institutions: Chair of Chemistry of Biogenic Resources, Technische Universität München Straubing, Germany, Institute of Fundamental Sciences, Massey University Palmerston North, New Zealand, The MacDiarmid Institute for Advanced Materials and Nanotechnology Palmerston North, New Zealand
  
   
  
  Pseudomonas
  CSDB ID 1099 (all data & tools)

Show legend Show as text

Structure type: oligomer

• Article ID: 510
  Zhang Z, Yu G, Guan H, Zhao X, Du Y, Jiang X "Preparation and structure elucidation of alginate oligosaccharides degraded by alginate lyase from Vibro sp. 510" - Carbohydrate Research 339(8) (2004) 1475-1481
  

  Alginate that was purified from the fermentation solution of marine bacteria Vibro sp. 510 under specific reaction conditions was hydrolyzed by alginate lyase. Seven oligosaccharides, including di-, tri- and tetrasaccharides, were isolated through low-pressure, gel-permeation chromatography (LP-GPC) and semipreparative strong-anion exchange (SAX) fast-protein liquid chromatography (FPLC). The oligosaccharide structures were elucidated based on ESIMS and 2D NMR spectral analysis. The hydrolytic specificity of this alginate lyase to alginate is discussed.

  Oligosaccharides, alginate, alginate lyase, guluronic acid, mannuronic acid

  NCBI PubMed ID: 15178390
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: glyu@mail.ouc.edu.cn
  Institutions: Institute of Marine Drug and Food, Ocean University of China, Qingdao, China, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China, Department of Food Science and Technology, Ocean University of China, Qingdao, China
  Methods: gel filtration, NMR-2D, enzymatic hydrolysis, ESI-MS, anion-exchange chromatography, fast protein chromatography
  
   
  
  (bacteria)
  CSDB ID 9471 (all data & tools)

Show legend Show as text

Structure type: oligomer

• Article ID: 510
  Zhang Z, Yu G, Guan H, Zhao X, Du Y, Jiang X "Preparation and structure elucidation of alginate oligosaccharides degraded by alginate lyase from Vibro sp. 510" - Carbohydrate Research 339(8) (2004) 1475-1481
  

  Alginate that was purified from the fermentation solution of marine bacteria Vibro sp. 510 under specific reaction conditions was hydrolyzed by alginate lyase. Seven oligosaccharides, including di-, tri- and tetrasaccharides, were isolated through low-pressure, gel-permeation chromatography (LP-GPC) and semipreparative strong-anion exchange (SAX) fast-protein liquid chromatography (FPLC). The oligosaccharide structures were elucidated based on ESIMS and 2D NMR spectral analysis. The hydrolytic specificity of this alginate lyase to alginate is discussed.

  Oligosaccharides, alginate, alginate lyase, guluronic acid, mannuronic acid

  NCBI PubMed ID: 15178390
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: glyu@mail.ouc.edu.cn
  Institutions: Institute of Marine Drug and Food, Ocean University of China, Qingdao, China, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China, Department of Food Science and Technology, Ocean University of China, Qingdao, China
  Methods: gel filtration, NMR-2D, enzymatic hydrolysis, ESI-MS, anion-exchange chromatography, fast protein chromatography
  
   
  
  (bacteria)
  CSDB ID 9472 (all data & tools)

Show legend Show as text

Structure type: oligomer

• Article ID: 510
  Zhang Z, Yu G, Guan H, Zhao X, Du Y, Jiang X "Preparation and structure elucidation of alginate oligosaccharides degraded by alginate lyase from Vibro sp. 510" - Carbohydrate Research 339(8) (2004) 1475-1481
  

  Alginate that was purified from the fermentation solution of marine bacteria Vibro sp. 510 under specific reaction conditions was hydrolyzed by alginate lyase. Seven oligosaccharides, including di-, tri- and tetrasaccharides, were isolated through low-pressure, gel-permeation chromatography (LP-GPC) and semipreparative strong-anion exchange (SAX) fast-protein liquid chromatography (FPLC). The oligosaccharide structures were elucidated based on ESIMS and 2D NMR spectral analysis. The hydrolytic specificity of this alginate lyase to alginate is discussed.

  Oligosaccharides, alginate, alginate lyase, guluronic acid, mannuronic acid

  NCBI PubMed ID: 15178390
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: glyu@mail.ouc.edu.cn
  Institutions: Institute of Marine Drug and Food, Ocean University of China, Qingdao, China, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China, Department of Food Science and Technology, Ocean University of China, Qingdao, China
  Methods: gel filtration, NMR-2D, enzymatic hydrolysis, ESI-MS, anion-exchange chromatography, fast protein chromatography
  
   
  
  (bacteria)
  CSDB ID 9473 (all data & tools)

Show legend Show as text

Structure type: oligomer

• Article ID: 510
  Zhang Z, Yu G, Guan H, Zhao X, Du Y, Jiang X "Preparation and structure elucidation of alginate oligosaccharides degraded by alginate lyase from Vibro sp. 510" - Carbohydrate Research 339(8) (2004) 1475-1481
  

  Alginate that was purified from the fermentation solution of marine bacteria Vibro sp. 510 under specific reaction conditions was hydrolyzed by alginate lyase. Seven oligosaccharides, including di-, tri- and tetrasaccharides, were isolated through low-pressure, gel-permeation chromatography (LP-GPC) and semipreparative strong-anion exchange (SAX) fast-protein liquid chromatography (FPLC). The oligosaccharide structures were elucidated based on ESIMS and 2D NMR spectral analysis. The hydrolytic specificity of this alginate lyase to alginate is discussed.

  Oligosaccharides, alginate, alginate lyase, guluronic acid, mannuronic acid

  NCBI PubMed ID: 15178390
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: glyu@mail.ouc.edu.cn
  Institutions: Institute of Marine Drug and Food, Ocean University of China, Qingdao, China, Research Center for Eco-Environmental Sciences, Chinese Academy of Sciences, Beijing 100085, China, Department of Food Science and Technology, Ocean University of China, Qingdao, China
  Methods: gel filtration, NMR-2D, enzymatic hydrolysis, ESI-MS, anion-exchange chromatography, fast protein chromatography
  
   
  
  (bacteria)
  CSDB ID 9474 (all data & tools)

Show legend Show as text

Structure type: structural motif or average structure
Trivial name: alginate
Compound class: polysaccharide

• Article ID: 839
  Jain S, Franklin MJ, Ertesvag H, Valla S, Ohman DE "The dual roles of AlgG in C-5-epimerization and secretion of alginate polymers in Pseudomonas aeruginosa" - Molecular Microbiology 47(4) (2003) 1123-1133
  

  Pseudomonas aeruginosa strains causing chronic pulmonary infections in cystic fibrosis patients produce high levels of alginate, an exopolysaccharide that confers a mucoid phenotype. Alginate is a linear polymer of d-mannuronate (M) and variable amounts of its C-5-epimer, l-guluronate (G). AlgG is a periplasmic C-5-epimerase that converts poly d-mannuronate to the mixed M+G sequence of alginate. To understand better the role and mechanism of AlgG activity, a mutant was constructed in the mucoid strain FRD1 with a defined non-polar deletion of algG. Instead of producing poly mannuronate, the algG deletion mutant secreted dialysable uronic acids, as does a mutant lacking the periplasmic protein AlgK. High levels of unsaturated ends and the nuclear magnetic resonance spectroscopy pattern revealed that the small, secreted uronic acids were the products of extensive polymer digestion by AlgL, a periplasmic alginate lyase co-expressed with AlgG and AlgK. Thus, AlgG is bifunctional with (i) epimerase activity and (ii) a role in protecting alginate from degradation by AlgL during transport through the periplasm. AlgK appears to share the second role. AlgG and AlgK may be part of a periplasmic protein complex, or scaffold, that guides alginate polymers to the outer membrane secretin (AlgE). To characterize the epimerase activity of AlgG further, the algG4 allele of poly mannuronate-producing FRD462 was shown to encode a protein lacking only the epimerase function. The sequence of algG4 has a Ser-272 to Asn substitution in a serine-threonine-rich and conserved region of AlgG, which revealed a critical residue for C-5-epimerase activity

  Pseudomonas aeruginosa, exopolysaccharide, epimerase, cystic fibrosis, alginate, alginate lyase, uronic acids

  NCBI PubMed ID: 12581364
  Publication DOI: 10.1046/j.1365-2958.2003.03361.x
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: deohman@hsc.vcu.edu
  Institutions: Department of Microbiology, Medical College of Virginia Campus of Virginia Commonwealth University, 1101 E. Marshall St., Rm. 5-051, Richmond, VA 23298-0678, USA, Department of Microbiology, Medical College of Virginia Campus of Virginia Commonwealth University, Richmond, USA
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 2591 (all data & tools)
• Article ID: 5505
  Stender EGP, Dybdahl Andersen C, Fredslund F, Holck J, Solberg A, Teze D, Peters GHJ, Christensen BE, Aachmann FL, Welner DH, Svensson B "Structural and functional aspects of mannuronic acid-specific PL6 alginate lyase from the human gut microbe Bacteroides cellulosilyticus" - Journal of Biological Chemistry 294(47) (2019) 17915-17930
  

  Alginate is a linear polysaccharide from brown algae consisting of 1,4-linked β-d-mannuronic acid (M) and α-l-guluronic acid (G) arranged in M, G, and mixed MG blocks. Alginate was assumed to be indigestible in humans, but bacteria isolated from fecal samples can utilize alginate. Moreover, genomes of some human gut microbiome-associated bacteria encode putative alginate-degrading enzymes. Here, we genome-mined a polysaccharide lyase family 6 alginate lyase from the gut bacterium Bacteroides cellulosilyticus (BcelPL6). The structure of recombinant BcelPL6 was solved by X-ray crystallography to 1.3 A resolution, revealing a single-domain, monomeric parallel beta-helix containing a 10-step asparagine ladder characteristic of alginate-converting parallel beta-helix enzymes. Substitutions of the conserved catalytic site residues Lys-249, Arg-270, and His-271 resulted in activity loss. However, imidazole restored the activity of BcelPL6-H271N to 2.5% that of the native enzyme. Molecular docking oriented tetra-mannuronic acid for syn attack correlated with M specificity. Using biochemical analyses, we found that BcelPL6 initially releases unsaturated oligosaccharides of a degree of polymerization of 2-7 from alginate and polyM, which were further degraded to di- and trisaccharides. Unlike other PL6 members, BcelPL6 had low activity on polyMG and none on polyG. Surprisingly, polyG increased BcelPL6 activity on alginate 7-fold. LC-electrospray ionization-MS quantification of products and lack of activity on NaBH4-reduced octa-mannuronic acid indicated that BcelPL6 is an endolyase that further degrades the oligosaccharide products with an intact reducing end. We anticipate that our results advance predictions of the specificity and mode of action of PL6 enzymes.

  crystal structure, alginate lyase, enzyme mutation, asparagine ladder, Bacteroides cellulolyticus, enzyme kinetics, enzyme mechanism, imidazole rescue, molecular docking, parallel beta-helix

  NCBI PubMed ID: 31530640
  Publication DOI: 10.1074/jbc.RA119.010206
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: bis@bio.dtu.dk
  Institutions: Department of Biotechnology and Biomedicine, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, DK-2800 Kgs. Lyngby, Denmark, Department of Biotechnology and Food Science, NTNU, Norwegian University of Science and Technology, N-7491 Trondheim, Norway
  Methods: PCR, X-ray, kinetics assays, enzymatic hydrolysis, MALDI-TOF MS, cloning, bioinformatic analysis, crystallization, SEC, LC-ESI-MS, binding assays, mutagenesis
  
   
  
  (bacteria)
  CSDB ID 1122 (all data & tools)
• Article ID: 12516
  Nagaoka M, Shibata H, Kimura-Takagi I, Hashimoto S, Aiyama R, Ueyama S, Yokokura T "Anti-ulcer effects and biological activities of polysaccharides from marine algae" - BioFactors 12(1-4) (2000) 267-274
  

  The nutritional value of marine algae has long been recognized in the Orient, but in the Western world, the use of seaweeds for human consumption is limited: they exist as additives and so-called health foods. In contrast, more seaweed than ever before is being eaten in Japan, China and Korea. Seaweeds are low in fats, and contain vitamins and minerals [1,2]. They also contain a large quantity of chemically characteristic mucilaginous polysaccharides such as agar, carrageenans, alginate, laminaran, rhamnan sulfate and fucoidan. These polysaccharides differ from those in terrestrial vegetables and provide dietary fiber: the human body does not digest them [3]. These polysaccharides are used in the food and pharmaceutical industries and have recently been demonstrated to have some unique biological activities. In this paper, we review the structure and function of marine algal polysaccharides, especially the anti-ulcer effect of fucoidan.

  polysaccharides, algae, anti-ulcer effects, seaweeds, fucoidan

  NCBI PubMed ID: 11216495
  Publication DOI: 10.1002/biof.5520120140
  Journal NLM ID: 8807441
  Publisher: Oxford; Washington, DC: IRL Press, International Union of Biochemistry
  Correspondence: masato-nagaoka@yakult.co.jp
  Institutions: Yakult Central Institute for Microbiological Research, Kunritachi, Japan
  
   
  
  (Phaeophyceae)
  CSDB ID 67024 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: CPS, EPS
Contained glycoepitopes: IEDB_130648,IEDB_137340,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_141807,IEDB_151531,IEDB_885822

• Article ID: 1131
  Rahman MM, Guard-Petter J, Asokan K, Hughes C, Carlson RW "The structure of the colony migration factor from pathogenic Proteus mirabilis - A capsular polysaccharide that facilitates swarming" - Journal of Biological Chemistry 274(33) (1999) 22993-22998
  

  Swarming by Proteus mirabilis is characterized by cycles of rapid and coordinated population migration across surfaces following differentiation of vegetative cells into elongated hyperflagellated swarm cells. It has been shown that surface colony expansion by the swarm cell population is facilitated by a colony migration factor (Cmf), a capsular polysaccharide (CPS) that also contributes to the uropathogenicity of P. mirabilis (Gygi, D., Rahman, M. M., Lai, H.-C., Carlson, R., Guard-Petter, J., and Hughes, C. (1995) Mol. Microbiol. 17, 1167-1175). In this report, the Cmf-CPS was extracted with hot water, precipitated with ethanol, and further purified by gel permeation chromatography. Its structure was established by glycosyl composition and linkage analyses, and by one- and two-dimensional NMR spectroscopy. The Cmf-CPS is composed of the following tetrasaccharide repeating unit. [see text]

  structure, capsular, polysaccharide, capsular polysaccharide, factor, Proteus, Proteus mirabilis, migration, pathogenic, swarming, colony

  NCBI PubMed ID: 10438465
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: rcarlson@ccrc.uga.edu
  Institutions: Complex Carbohydrate Research Center, The University of Georgia, Athens, GA, USA, Southeast Poultry Research Laboratory, United States Department of Agriculture, Agricultural Research Service, Athens, Georgia 30605, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, United Kingdom
  Methods: 13C NMR, 1H NMR, GLC-MS, NMR-2D, DOC-PAGE
  
   
  
  Proteus mirabilis WT19 (U6450), Proteus mirabilis WT19 (proticine P3/S1)
  CSDB ID 4309 (all data & tools)
• Article ID: 5791
  Knirel YA, Van Calsteren M "Bacterial exopolysaccharides" - Book: Comprehensive Glycoscience: From Chemistry to Systems Biology. Reference Module in Chemistry, Molecular Sciences and Chemical Engineering (2021) 1-75
  

  Bacterial extracellular polysaccharides are known as a cell-bound capsule, a sheath, or a slime, which is excreted into the environment. They play an important role in virulence of medical bacteria and plant-to-symbiont interaction and are used for serotyping of bacteria and production of vaccines. Some exopolysaccharides have commercial applications in industry, and claims of health benefits have been documented for an increasing number of them. Exopolysaccharides have diverse composition and structure, and some contain sugar and non-sugar components that are found in bacterial carbohydrates only. The present article provides an updated collection of the data on exopolysaccharides of various classes of gram-negative and gram-positive bacteria reported until the end of 2019. When known, biosynthesis pathways of exopolysaccharides are treated in a summary manner. References are made to structure and biosynthesis relatedness between exopolysaccharides of different bacterial taxa as well as between bacterial polysaccharides and mammalian glycosaminoglycans.

  polysaccharide structure, Gram-negative bacteria, capsule, Biofilm, polysaccharide biosynthesis, gram-positive bacteria, Monosaccharide composition, Bacterial exopolysaccharide, non-sugar component

  Publication DOI: 10.1016/B978-0-12-819475-1.00005-5
  Publisher: Elsevier
  Correspondence: marie-rose.vancalsteren@canada.ca; yknirel@gmail.com
  Editors: Barchi J, Kamerling H
  Institutions: N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Saint-Hyacinthe Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, QC, Canada
  
   
  
  Proteus mirabilis WT19
  CSDB ID 4286 (all data & tools)

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Structure type: polymer chemical repeating unit
Trivial name: alginate

• Article ID: 1620
  Herasimenka Y, Benincasa M, Mattiuzzo M, Cescutti P, Gennaro R, Rizzo R "Interaction of antimicrobial peptides with bacterial polysaccharides from lung pathogens" - Peptides 26(7) (2005) 1127-1132
  

  The interaction of two cathelicidin antimicrobial peptides, LL-37 and SMAP-29, with three bacterial polysaccharides, respectively, produced by Pseudomonas aeruginosa, Burkholderia cepacia and Klebsiella pneumoniae, was investigated to identify possible mechanisms adopted by lung pathogens to escape the action of innate immunity effectors. In vitro assays indicated that the antibacterial activity of both peptides was inhibited to a variable extent by the three polysaccharides. Circular dichroism experiments showed that these induced an alpha-helical conformation in the two peptides, with the polysaccharides from K. pneumoniae and B. cepacia showing, respectively, the highest and the lowest effect. Fluorescence measurements also indicated the presence of peptide-polysaccharide interactions. A model is proposed in which the binding of peptides to the polysaccharide molecules induces, at low polysaccharide to peptide ratios, a higher order of aggregation, due to peptide-peptide interactions. Overall, these results suggest that binding of the peptides by the polysaccharides produced by lung pathogens can contribute to the impairment of peptide-based innate defenses of airway surface

  conformation, chemistry, Bacterial, microbiology, pathogenicity, Non-U.S.Gov't, polysaccharide, Burkholderia, Burkholderia cepacia, Pseudomonas, Pseudomonas aeruginosa, molecule, antigens, Carbohydrate Sequence, induced, Molecular Sequence Data, Klebsiella, Bacterial polysaccharide, activity, polysaccharides, mechanism, biochemistry, biophysics, surface, interaction, immunity, pathogen, pathogens, Klebsiella pneumoniae, bacterial polysaccharides, binding, measurement, action, effect, peptides, pneumonia, fluorescence, variable, assay, model, order, in vitro, defense, innate immunity, peptide, circular dichroism, pharmacology, macromolecular, Humans, Research Support, antimicrobial, aggregation, lung, antagonists & inhibitors, antibacterial, Antimicrobial Cationic Peptides, Blood Proteins

  NCBI PubMed ID: 15949630
  Journal NLM ID: 8008690
  Publisher: New York, NY: Elsevier
  Institutions: Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Licio Giorgieri 1, 34127 Trieste, Italy
  Methods: CD
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 10791 (all data & tools)

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Structure type: oligomer
Trivial name: alginate, mannuronan, guluronan
Compound class: EPS, alginate

• Article ID: 233
  Fett WF, Wells JM, Cescutti P, Wijey C "Identification of exopolysaccharides produced by fluorescent pseudomonads associated with commercial mushroom (Agaricus bisporus) production" - Applied and Environmental Microbiology 61 (1995) 513-517
  

  The acidic exopolysaccharides (EPSs) from 63 strains of mushroom production-associated fluorescent pseudomonads which were mucoid on Pseudomonas agar F medium (PAF) were isolated, partially purified, and characterized. The strains were originally isolated from discolored lesion which developed postharvest on mushroom (Agaricus bisporus) caps or from commercial lots of mushroom casing medium. An acidic galactoglucan, previously named marginalan, was produced by mucoid strains of the saprophyte Pseudomonas putida and the majority of mucoid strains of saprophytic P. fluorescens (biovars III and V) isolated from casing medium. One biovar II strain (J1) of P. fluorescens produced alginate, a copolymer of mannuronic and guluronic acids, and one strain (H13) produced an apparently unique EPS containing neutral and amino sugars. Of 10 strains of the pathogen "P. gingeri," the causal agent of mushroom ginger blotch, 8 gave mucoid growth on PAF. The "P. gingeri" EPS also was unique in containing both neutral sugar and glucuronic acid. Mucoid, weakly virulent strains of "P. reactans" produced either alginate or marginalan. All 10 strains of the pathogen P. tolaasii, the causal agent of brown blotch of mushrooms were nonnmucoid on PAF. Production of EPS by these 10 strains plus the 2 nonmucoid strains of "P. gingeri" also was negative on several additional solid media as well as in two broth media tested. The results support our previous studies indicating that fluorescent pseudomonads are a rich source of novel EPSs.

  Pseudomonas, exopolysaccharide, exopolysaccharides, identification, production, fluorescent, mushroom

  NCBI PubMed ID: 7574589
  Journal NLM ID: 7605801
  Publisher: American Society for Microbiology
  Institutions: Eastern Regional Research Center, U.S. Department of Agriculture, Philadelphia, Pennsulvania 19118, USA, Departement of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Trieste, Italy
  
   
  
  Pseudomonas fluorescens, Pseudomonas reactans
  CSDB ID 104006 (all data & tools)
• Article ID: 1699
  Leitão JH, Sá-Correia I "Growth-phase-dependent alginate synthesis, activity of biosynthetic enzymes and transcription of alginate genes in Pseudomonas aeruginosa" - Archives of Microbiology 163 (1995) 217-222
  

  Alginate synthesis by the highly mucoid Pseudomonas aeruginosa 8821 M is growth-phase-dependent, and the alginate produced per unit of biomass reaches maximum values in the deceleration phase of growth. However, the degree of polymerization increases as batch growth proceeds, reaching maximum values at the stationary phase of growth. The activity of the four enzymes leading to GDP-mannuronic acid formation, phosphomannose isomerase, phosphomannomutase, GDP-mannose pyrophosphorylase and GDP-mannose dehydrogenase peaked earlier at the late exponential phase. Growth-phase-dependent activity of alginate biosynthetic enzymes correlates with the level of transcription of the encoding alginate genes algA, algC and algD during growth, as indicated by Northern blot hybridization experiments. The pattern of coordinate transcriptional growth-phase regulation of these alginate structural genes concurs with the growth-dependent transcription of the regulatory gene algR1.

  Pseudomonas aeruginosa, regulation, exopolysaccharides, alginate, Alginate enzymes, Growth-phase, Alginate genes algA, algC, algD, algR1

  NCBI PubMed ID: 7778978
  Publication DOI: 10.1007/BF00305356
  Journal NLM ID: 0410427
  Publisher: Berlin, New York: Springer
  Institutions: Laboratório de Engenharia Bioquímica, Instituto Superior Técnico, Lisboa, Portugal
  
   
  
  Pseudomonas aeruginosa 8821 M
  CSDB ID 105075 (all data & tools)
• Article ID: 2488
  Malissard M, Duez C, Guinand M, Vacheron MJ, Michel G, Marty N, Joris B, Thamm I, Ghuysen JM "Sequence of a gene encoding a (poly ManA) alginate lyase active on Pseudomonas aeruginosa alginate" - FEMS Microbiology Letters 110 (1993) 101-106
  

  The recombinant plasmid pAL-A3 bears a (poly ManA) alginate lyase-encoding gene that originates from the marine bacterium ATCC 433367 (Brown et al., Appl. Environ. Microbiol. (1991) 57, 1870-1872). The alginate lyase produced by Escherichia coli TC4 harbouring pAL-A3 was purified to protein homogeneity and the corresponding gene sequenced, giving access to the first known primary structure of an alginate lyase. The 265-amino acid residue alginate lyase showed lytic activity on a Pseudomonas aeruginosa alginate isolated from a cystic fibrosis patient. Unexpectedly, the alginate lyase thus characterized differed from that isolated from the culture medium of the bacterium ATCC 433367 (Romeo and Preston, Biochemistry (1986) 25, 8385-8391).

  NCBI PubMed ID: 8319887
  Journal NLM ID: 7705721
  Publisher: Blackwell Publishing
  Institutions: Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, Villeurbanne, France
  
   
  
  Laminaria hyperborea, Macrocystis pyrifera, Pseudomonas aeruginosa
  CSDB ID 126035 (all data & tools)
• Article ID: 2493
  Malissard M, Chavagnat F, Duez C, Vacheron MJ, Guinand M, Michel G, Ghuysen JM "Overproduction and properties of the mannuronate alginate lyase AlxMB" - FEMS Microbiology Letters 126 (1995) 105-111
  

  In previous studies (Malissard et al., FEMS Microbiol. Lett. (1993) 110, 101-106), the alginate lyase AlxM of the marine bacterium ATCC 433367 was produced in Escherichia coli TC4/pAL-A3 with a yield of 50 micrograms per litre of culture. The polypeptide chain was cleaved between two cysteine residues, C169 and C183, themselves linked by a disulphide bridge. AlxM has now been overproduced in E. coli BL21(DE3)/pAL-Sur/pLysS. Under conditions in which formation of inclusion bodies can be avoided, the enzyme is synthesized as a catalytically active, water-soluble, unnicked polypeptide with a yield of 32 mg per litre of culture. It has been purified to protein homogeneity using a one-step procedure. The nicked AlxMA and unnicked AlxMB alginate lyases have identical alginate-degrading activities at high salt concentrations.

  NCBI PubMed ID: 7705601
  Journal NLM ID: 7705721
  Publisher: Blackwell Publishing
  Institutions: Laboratoire de Biochimie Microbienne, Université Claude Bernard Lyon 1, Villeurbanne, France
  
   
  
  Laminaria hyperborea, Macrocystis pyrifera, Pseudomonas aeruginosa
  CSDB ID 126049 (all data & tools)
• Article ID: 2749
  Kumon H, Tomochika KI, Matunaga T, Ogawa M, Ohmori H "A sandwich cup method for the penetration assay of antimicrobial agents through Pseudomonas exopolysaccharides" - Microbiology and Immunology 38 (1994) 615-619
  

  We developed new sandwich cup method to assay the penetration of various antimicrobial agents through Pseudomonas exopolysaccharides. Using alginate extracted from mucoid-type Pseudomonas aeruginosa and gellan gum from Pseudomonas elodea, the role of exopolysaccharides as a barrier against drug penetration was examined. The penetration of positively charged hydrophilic drugs such as aminoglycosides and polypeptides was markedly inhibited by the gels tested, but that of beta-lactams, quinolones, and macrolides was not inhibited. The penetration of gentamicin was strongly influenced by the gel concentration, the solution to be used, and the presence of Ca2+. These results suggest that the microenvironment at the infection site could greatly influence drug penetration through biofilms in vivo.

  NCBI PubMed ID: 7799834
  Journal NLM ID: 7703966
  Publisher: Japanese Society For Bacteriology
  Institutions: Department of Urology, Okayama University Medical School, Japan
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 143609 (all data & tools)
• Article ID: 2751
  Sutherland IW "Industrially useful microbial polysaccharides" - Microbiological Sciences 3 (1986) 5-9
  

  A number of microbial exopolysaccharides possess properties of industrial importance, especially as viscosifiers and gelling agents. This group of biopolymers is diverse in its chemical composition and structure; it includes both anionic and neutral polysaccharides, most of which are of bacterial origin.

  mannuronan

  NCBI PubMed ID: 3153140
  Journal NLM ID: 8510101
  Institutions: Department of Microbiology, Edinburgh University, UK
  
   
  
  Azotobacter vinelandii, Pseudomonas aeruginosa
  CSDB ID 143641 (all data & tools)
• Article ID: 2774
  Shinabarger D, May TB, Boyd A, Ghosh M, Chakrabarty AM "Nucleotide sequence and expression of the Pseudomonas aeruginosa algF gene controlling acetylation of alginate" - Molecular Microbiology 9 (1993) 1027-1035
  
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 144067 (all data & tools)
• Article ID: 3043
  Rehm BHA, Grabert E, Hein J, Winkler UK "Antibody response of rabbits and cystic fibrosis patients to an alginate-specific outer membrane protein of a mucoid strain of Pseudomonas aeruginosa" - Microbial Pathogenesis 16 (1994) 43-51
  

  The aim of this work was to study the immunogenicity of an outer membrane (OM) protein (AlgE; 54 kDa) which is produced solely by mucoid, i.e. alginate-producing strains of P. aeruginosa. The source of AlgE used for our study was the mucoid strain CF3/M1 originally isolated from sputum of a cystic fibrosis (CF) patient. The purified non-denatured protein served as antigen to raise polyclonal monospecific anti-AlgE antibodies in rabbits and to assay sera from 41 cystic fibrosis (CF) patients for anti-AlgE antibodies. According to clinical protocols the sputa of 22 CF patients were positive for P. aeruginosa, 18 were negative and one case was unknown. Our ELISA studies showed that high titers of anti-AlgE antibodies (IgG) corresponded well with the infection status of the CF patients. None of 23 control sera derived from healthy volunteers contained significant levels of anti-AlgE antibodies. Thus the ELISA should be considered as a sensitive diagnostic tool for the early detection of mucoid P. aeruginosa infections in CF patients. Furthermore, we suggest to include AlgE in a multicomponent experimental vaccine for potential protection of non-colonized CF patients from colonization with mucoid P. aeruginosa.

  Bacterial, antibody response, cystic fibrosis, alginate, outer membrane protein, mucoid bacteria

  NCBI PubMed ID: 8057826
  Journal NLM ID: 8606191
  Publisher: Academic Press
  Institutions: Ruhr-Universität Bochum, Lehrstuhl für Biologie der Mikroorganismen, Germany
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 143569 (all data & tools)
• Article ID: 3118
  Pier GB, DesJardin D, Grout M, Garner C, Bennett SE, Pekoe G, Fuller SA, Thornton MO, Harkonen WS, Miller HC "Human immune response to Pseudomonas aeruginosa mucoid exopolysaccharide (alginate) vaccine" - Infection and Immunity 62(9) (1994) 3972-3979
  

  Chronic lung infection with mucoid Pseudomonas aeruginosa is the major pathologic feature of cystic fibrosis. Previous studies suggested that a failure to produce opsonic antibody to the mucoid exopolysaccharide (MEP; also called alginate) capsule is associated with the maintenance of chronic bacterial infection. Provision of MEP-specific opsonic antibodies has therapeutic potential. To evaluate the ability of MEP to elicit opsonic antibodies, humans were immunized with two lots of MEP vaccine that differed principally in molecular size. Lot 2 had a larger average MEP polymer size. Both vaccines were well tolerated, but lot 1 was poorly immunogenic, inducing long-lived opsonic antibodies in only 2 of 28 vaccinates given doses of 10 to 150 micrograms. In contrast, at the optimal dose of 100 micrograms, lot 2 elicited long-lived opsonic antibodies in 80 to 90% of the vaccinates. The antibodies elicited by both lots enhanced deposition of C3 onto mucoid P. aeruginosa cells and mediated opsonic killing of heterologous mucoid strains expressing distinct MEP antigens. These results indicate that the polymers of MEP with the largest molecular sizes safely elicit opsonic antibodies in a sufficiently large proportion of vaccinates to permit studies of active and passive immunization of cystic fibrosis patients against infection with mucoid P. aeruginosa.

  NCBI PubMed ID: 8063415
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Channing Laboratory, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115
  Methods: ELISA
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 130563 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: EPS
Contained glycoepitopes: IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_151528,IEDB_190606,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 1915
  Sloneker JH, Orentas DG, Knutson CA, Watson PR, Jeanes A "Structure of the extracellular bacterial polysaccharide from Arthrobacter viscosus NRRL B-1973" - Canadian Journal of Chemistry 46(21) (1968) 3353-3361
  

  D-Glucose, D-galactose, and D-mannuronic acid in equimolar proportions constitute 75% of the weight of the polysaccharide elaborated by Arthrobacter viscosus NRRL B-1973. O-Acetyl groups account for the remaining 25% of the weight; 50% of the hydroxyl groups are acetylated. Acid hydrolysis of the polysaccharide revealed that the D-mannopyranosyluronic acid bonds hydrolyzed with unexpected ease. Controlled acid hydrolysis afforded three oligosaccharides identified as 4-O-β-D-glucopyranosyl-D-galactose; 4-O-β-D-mannopyranosyluronic acid-D-glucose; and O-β-D-mannopyranosyluronic acid-(1 → 4)-O-β-D-glucopyranosyl-(1 → 4)-D-galactose. The native polysaccharide was oxidized slowly by sodium metaperiodate and consumed 0.42 mole per sugar residue in 340 h at 4°. The deacetylated polysaccharide consumed 0.67 mole of periodate per sugar residue and produced 1 mole of acid per 160 to 165 sugar residues in 170 h at 4°. At 20° the deacetylated polysaccharide was oxidized excessively by periodate, 1.5 moles of oxidant was consumed, and 0.4 mole of acid was produced per sugar residue in 340 h. However, only 20% of the C4-substituted D-glucose residues in the polysaccharide was cleaved by periodate in spite of the excessive oxidation at 20°.The polysaccharide has a linear structure and consists predominantly of repeating trisaccharide units, O-β-D-mannopyranosyluronic acid-(1 → 4)-O-β-D-glucopyranosyl-(1 → 4)-D-galactose.

  Publication DOI: 10.1139/v68-552
  Journal NLM ID: 0372705
  Publisher: National Research Council of Canada Canada
  Institutions: Northern Regional Research Laboratory, Northern Utilization Research and Development Division, Agricultural Research Service, Utrited States Department of Agriculture, Peoria, Illinois 61604
  Methods: methylation, partial acid hydrolysis, sugar analysis, TLC, GLC, paper chromatography, de-O-acetylation, ion-exchange chromatography, optical rotation measurement, periodate borohydride reduction
  
   
  
  Arthrobacter viscosus
  CSDB ID 112157 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Compound class: EPS
Contained glycoepitopes: IEDB_136044,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_190606,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

• Article ID: 1915
  Sloneker JH, Orentas DG, Knutson CA, Watson PR, Jeanes A "Structure of the extracellular bacterial polysaccharide from Arthrobacter viscosus NRRL B-1973" - Canadian Journal of Chemistry 46(21) (1968) 3353-3361
  

  D-Glucose, D-galactose, and D-mannuronic acid in equimolar proportions constitute 75% of the weight of the polysaccharide elaborated by Arthrobacter viscosus NRRL B-1973. O-Acetyl groups account for the remaining 25% of the weight; 50% of the hydroxyl groups are acetylated. Acid hydrolysis of the polysaccharide revealed that the D-mannopyranosyluronic acid bonds hydrolyzed with unexpected ease. Controlled acid hydrolysis afforded three oligosaccharides identified as 4-O-β-D-glucopyranosyl-D-galactose; 4-O-β-D-mannopyranosyluronic acid-D-glucose; and O-β-D-mannopyranosyluronic acid-(1 → 4)-O-β-D-glucopyranosyl-(1 → 4)-D-galactose. The native polysaccharide was oxidized slowly by sodium metaperiodate and consumed 0.42 mole per sugar residue in 340 h at 4°. The deacetylated polysaccharide consumed 0.67 mole of periodate per sugar residue and produced 1 mole of acid per 160 to 165 sugar residues in 170 h at 4°. At 20° the deacetylated polysaccharide was oxidized excessively by periodate, 1.5 moles of oxidant was consumed, and 0.4 mole of acid was produced per sugar residue in 340 h. However, only 20% of the C4-substituted D-glucose residues in the polysaccharide was cleaved by periodate in spite of the excessive oxidation at 20°.The polysaccharide has a linear structure and consists predominantly of repeating trisaccharide units, O-β-D-mannopyranosyluronic acid-(1 → 4)-O-β-D-glucopyranosyl-(1 → 4)-D-galactose.

  Publication DOI: 10.1139/v68-552
  Journal NLM ID: 0372705
  Publisher: National Research Council of Canada Canada
  Institutions: Northern Regional Research Laboratory, Northern Utilization Research and Development Division, Agricultural Research Service, Utrited States Department of Agriculture, Peoria, Illinois 61604
  Methods: methylation, partial acid hydrolysis, sugar analysis, TLC, GLC, paper chromatography, de-O-acetylation, ion-exchange chromatography, optical rotation measurement, periodate borohydride reduction
  
   
  
  Arthrobacter viscosus
  CSDB ID 620 (all data & tools)
• Article ID: 5791
  Knirel YA, Van Calsteren M "Bacterial exopolysaccharides" - Book: Comprehensive Glycoscience: From Chemistry to Systems Biology. Reference Module in Chemistry, Molecular Sciences and Chemical Engineering (2021) 1-75
  

  Bacterial extracellular polysaccharides are known as a cell-bound capsule, a sheath, or a slime, which is excreted into the environment. They play an important role in virulence of medical bacteria and plant-to-symbiont interaction and are used for serotyping of bacteria and production of vaccines. Some exopolysaccharides have commercial applications in industry, and claims of health benefits have been documented for an increasing number of them. Exopolysaccharides have diverse composition and structure, and some contain sugar and non-sugar components that are found in bacterial carbohydrates only. The present article provides an updated collection of the data on exopolysaccharides of various classes of gram-negative and gram-positive bacteria reported until the end of 2019. When known, biosynthesis pathways of exopolysaccharides are treated in a summary manner. References are made to structure and biosynthesis relatedness between exopolysaccharides of different bacterial taxa as well as between bacterial polysaccharides and mammalian glycosaminoglycans.

  polysaccharide structure, Gram-negative bacteria, capsule, Biofilm, polysaccharide biosynthesis, gram-positive bacteria, Monosaccharide composition, Bacterial exopolysaccharide, non-sugar component

  Publication DOI: 10.1016/B978-0-12-819475-1.00005-5
  Publisher: Elsevier
  Correspondence: marie-rose.vancalsteren@canada.ca; yknirel@gmail.com
  Editors: Barchi J, Kamerling H
  Institutions: N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Saint-Hyacinthe Research and Development Centre, Agriculture and Agri-Food Canada, Saint-Hyacinthe, QC, Canada
  
   
  
  Arthrobacter viscosus NRRL B-1973
  CSDB ID 25125 (all data & tools)

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Structure type: polymer chemical repeating unit
Compound class: EPS

• Article ID: 2201
  Likhosherstov LM, Senchenkova SN, Shashkov AS, Derevitskaya VA, Danilova IV, Botvinko IV "Structure of the major exopolysaccharide produced by Azotobacter beijerinckii B-1615" - Carbohydrate Research 222 (1991) 233-238
  

  A. beijerinckii strain B-1615 produced two acidic exopolysaccharides in the ratio approximately 9:1. The minor polysaccharide contained mannuronic and guluronic acids in the ratio 2.3:1 and is a bacterial alginate. The major polysaccharide consisted of D-galactose, L-rhamnose, and pyruvic acid in the ratios 2:1:1 and was acetylated. On the basis of methylation analysis, and 1H- and 13C-n.m.r. spectroscopy of the polysaccharide before and after removal of the pyruvic acid residues and O-deacetylation, it was concluded that the major polysaccharide had the structure [formula; see text] with up to 1.5 OAc groups per repeating unit.

  NCBI PubMed ID: 1813106
  Publication DOI: 10.1016/0008-6215(91)89021-7
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Academy of Sciences of the U.S.S.R., Moscow
  Methods: 13C NMR, 1H NMR, GLC, chemical methods
  
   
  
  Azotobacter beijerinckii
  CSDB ID 116381 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: the Macrocystis pyrifera alginate is comprised of 60% 4-linked ManA and 40% 4-linked GulA residues, the Pseudomonas aeruginosa alginate is comprised of 80% 4-linked ManA and 20% 4-linked GulA residues

• Article ID: 2208
  Zeller SG, Gray GR "Analysis of Macrocystis pyrifera and Pseudomonas aeruginosa alginic acids by the reductive-cleavage method" - Carbohydrate Research 226 (1992) 313-326
  

  Permethylated alginic acids comprised of 4-linked D-mannopyranosyluronic acid and 4-linked L-gulopyranosyluronic acid residues undergo reductive cleavage to yield, after acetylation, methyl 3-O-acetyl-2,6-anhydro-4,5-di-O-methyl-D-mannonate (2b) and methyl 3-O-acetyl-2,6-anhydro-4,5-di-O-methyl-D-gluconate (3b) as major products. Small amounts (ca. 13%) of ring-contracted products, namely methyl 2-O-acetyl-3,6-anhydro-4,5-di-O-methyl-D-mannonate (9) and methyl 2-O-acetyl-3,6-anhydro-4,5-di-O-methyl-D-gluconate (10), were also observed in these experiments. These results are in marked contrast to previous results on the reductive cleavage of 4-linked D-glucopyranosyluronic acid residues, wherein the ring-contracted product was formed exclusively. Formation of the ring-contracted products could be completely eliminated by reduction (LiAlH4) of ester groups in the permethylated alginic acid prior to reductive cleavage. In the latter experiments, 4,6-di-O-acetyl-1,5-anhydro-2,3-di-O-methyl-D-mannitol (5b) and 4,6-di-O-acetyl-1,5-anhydro-2,3-di-O-methyl-L-gulitol (6b) were the sole products of reductive cleavage of the 4-linked ManA and 4-linked GulA residues, respectively. However, in the previous experiments it was noted that low yields of permethylated alginic acids were obtained and that extensive depolymerization occurred under methylation conditions. Depolymerization could be avoided and higher yields of permethylated polysaccharides could be obtained, by reduction of the carboxyl groups of the alginic acids prior to methylation. Reductive cleavage of the latter polysaccharides yielded the products expected from 4-linked D-mannopyranosyl and 4-linked L-gulopyranosyl residues, namely 4-O-acetyl-1,5-anhydro-2,3,6-tri-O-methyl-D-mannitol (13b) and 4-O-acetyl-1,5-anhydro-2,3,6-tri-O-methyl-L-gulitol (14b), respectively. Using the latter analytical strategy, it was established that the Macrocystis pyrifera alginate was comprised of 60% 4-linked ManA and 40% 4-linked GulA residues, whereas the Pseudomonas aeruginosa alginate was comprised of 80% 4-linked ManA and 20% 4-linked GulA residues.

  NCBI PubMed ID: 1617691
  Publication DOI: 10.1016/0008-6215(92)84079-8
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Chemistry, University of Minnesota, Minneapolis 55455.
  
   
  
  Macrocystis pyrifera, Pseudomonas aeruginosa
  CSDB ID 116582 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: EPS

• Article ID: 2801
  Pier GB "Vaccine potential of Pseudomonas aeruginosa mucoid exopolysaccharide (Alginate)" - Proceedings of Pseudomonas aeruginosa in human diseases. International Symposium on Basic Research and Clinical Aspects of Pseudomonas Aeruginosa Infection (3rd : 1990 : Tokyo, Japan) (1991) Vol. 44, 136-142
  
  Book NLM ID: 9109304
  Publisher: Basel, New York : Karger
  Editors: Homma JY et al.
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 147989 (all data & tools)