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: homopolymer
Trivial name: alginate, guluronan
Compound class: polysaccharide

• 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 8407 (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 116487 (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 143639 (all data & tools)
• Article ID: 2899
  Boyd A, Chakrabarty AM "Role of alginate lyase in cell detachment of Pseudomonas aeruginosa" - Applied and Environmental Microbiology 60 (1994) 2355-2359
  

  The exopolysaccharide alginate of Pseudomonas aeruginosa was shown to be important in determining the degree of cell detachment from an agar surface. Nonmucoid strain 8822 gave rise to 50-fold more sloughed cells than mucoid strains 8821 and 8830. Alginate anchors the bacteria to the agar surface, thereby influencing the extent of detachment. The role of the P. aeruginosa alginate lyase in the process of cell sloughing was investigated. Increased expression of the alginate lyase in mucoid strain 8830 led to alginate degradation and increased cell detachment. Similar effects were seen both when the alginate lyase was induced at the initial stage of cell inoculation and when it was induced at a later stage of growth. It appears that high-molecular-weight alginate polymers are required to efficiently retain the bacteria within the growth film. When expressed from a regulated promoter, the alginate lyase can induce enhanced sloughing of cells because of degradation of the alginate. This suggests a possible role for the lyase in the development of bacterial growth films.

  NCBI PubMed ID: 8074516
  Journal NLM ID: 7605801
  Publisher: American Society for Microbiology
  Institutions: Department of Microbiology and Immunology, University of Illinois College of Medicine, Chicago 60612
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 104000 (all data & tools)
• Article ID: 2967
  Lebrun L, Junter GA, Jouenne T, Mignot L "Exopolysaccharide production by free and immobilized microbial cultures" - Enzyme and Microbial Technology 16 (1994) 1048-1054
  

  The batch production of different exopolysaccharides (alginate, xanthan, pullulan, dextran) by free and immobilized microbial cultures was investigated. First, conventional free-cell cultures were performed to obtain control fermentation parameters and macromolecular characteristics of exopolysaccharides. Then microbial cultures were immobilized in composite agar layer/microporous membrane structures and tested for polysaccharide production. The immobilized-cell system proved unsuitable for xanthan and pullulan production. Owing to the fouling of the microporous membrane by the polysaccharide, dextran production by immobilized Leuconostoc mesenteroides also was inefficient. More promising results have been obtained with immobilized Azotobacter vinelandii cultures. The amount of alginate produced by immobilized A. vinelandii represented about 60% of that recovered from a free-cell culture, whereas the polysaccharide yield reached 35% instead of 9% for the free counterpart. These results are compared to the macromolecular characteristics of exopolysaccharides.

  Publication DOI: 10.1016/0141-0229(94)90141-4
  Journal NLM ID: 8003761
  Institutions: Equipe de Technologie Microbienne, URA 500 du CNRS, Université de Rouen, France
  
   
  
  Azotobacter vinelandii
  CSDB ID 122343 (all data & tools)
• Article ID: 3003
  Johansen HK, Espersen F, Cryz SJ, Hougen HP, Fomsgaard A, Rygaard J, Hoiby N "Immunization with Pseudomonas aeruginosa vaccines and adjuvant can modulate the type of inflammatory response subsequent to infection" - Infection and Immunity 62 (1994) 3146-3155
  

  Pseudomonas aeruginosa is the predominant pathogen in patients with cystic fibrosis (CF). To study the possibility of preventing lung inflammation and decreasing the progression of the infection by vaccination, we have developed a rat model of chronic P. aeruginosa lung infection. Rats were immunized with P. aeruginosa whole-cell sonicates, O-polysaccharide toxin A conjugate, an alginate-toxin A conjugate, or native alginate. Control animals received sterile saline or incomplete Freund's adjuvant (IFA). The macroscopic (mean score, 2.4 versus 2.7 to 3.2) (P < 0.05) and microscopic (mean score, 2.0 versus 2.1 to 2.8) pathologic abnormalities were less severe in the control rats injected with sterile saline than in the immunized rats and the IFA group. The more severe lung abnormalities observed in immunized rats could be due to the result of immune complex-mediated lung tissue damage. The histopathologic results in the saline control rats were characterized by acute inflammation dominated by numerous polymorphonuclear leukocytes surrounding the alginate beads (microcolonies), as in CF patients. In contrast, the inflammatory response in the IFA group and in the immunized rats had changed from an acute-type inflammation to a chronic-type inflammation dominated by mononuclear leukocytes and scattered granulomas. Cross-reacting antibodies were induced by the two alginate vaccines, and most immunized animals developed a significant (P < 0.001) antibody titer elevation (in enzyme-linked immunosorbent assay) of the immunoglobulin M (IgM), IgG, and IgA classes against the homologous antigens. The bacterial clearance was significantly (P < 0.05) more efficient in most immunized rats than in the control rats given sterile saline. The present study shows that none of the vaccines could completely prevent chronic lung inflammation 4 weeks after challenge. However, the changed pathologic condition in immunized rats to a chronic-type inflammation might be of great benefit in future management of CF patients since the developing lung tissue damage has been shown to be caused by polymorphonuclear leukocyte-released elastase.

  NCBI PubMed ID: 8039883
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Institutions: Department of Clinical Microbiology, Rigshospitalet, Copenhagen, Denmark
  
   
  
  Pseudomonas aeruginosa
  CSDB ID 130555 (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 67023 (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: structural motif or average structure
Trivial name: fucoidan
Compound class: polysaccharide
Contained glycoepitopes: IEDB_136045,IEDB_142489,IEDB_144562,IEDB_152214,IEDB_174333,SB_86

• 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 67026 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit
Trivial name: fucoidan
Compound class: polysaccharide
Contained glycoepitopes: IEDB_136045,IEDB_142489,IEDB_144562,IEDB_152214,IEDB_174333,SB_86

• 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 67027 (all data & tools)