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Structure type: suggested polymer biological repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_142489,IEDB_144562,IEDB_144990,IEDB_147450,IEDB_150767,IEDB_150948,IEDB_151528,IEDB_152214,IEDB_153553,IEDB_167071,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461711,IEDB_461719,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_25,SB_7,SB_8,SB_86,SB_88

• Article ID: 266
  Inamori K, Saito T, Iwaki D, Nagira T, Iwanaga S, Arisaka F, Kawabata S "A newly identified horseshoe crab lectin with specificity for blood group A antigen recognizes specific O-antigens of bacterial lipopolysaccharides" - Journal of Biological Chemistry 274(6) (1999) 3272-3278
  

  14-kDa lectin, named tachylectin-3, was newly identified from hemocytes of the Japanese horseshoe crab, Tachypleus tridentatus. This lectin exhibited hemagglutinating activity against human A-type erythrocytes, but not against the B- and O-types of erythrocytes and animal erythrocytes, including those of sheep, rabbit, horse, and bovine. The hemagglutinating activity of tachylectin-3 was equivalent to that of a previously identified lectin, named tachylectin-2, with affinity for N-acetyl-D-glucosamine or N-acetyl-D-galactosamine. However, the activity of tachylectin-3 was not inhibited by these two N-acetylhexosamines at 100 mM but was inhibited by a blood group A-pentasaccharide at a minimum inhibitory concentration of 0.16 mM. Furthermore, the hemagglutinating activity was strongly inhibited by bacterial S-type lipopolysaccharides (LPSs) from Gram-negative bacteria but not by R-type LPSs lacking O-antigens. One of the most effective S-type LPSs was from Escherichia coli O111:B4, with a minimum inhibitory concentration of 6 ng/ml. These data suggest that tachylectin-3 specifically recognizes Gram-negative bacteria through the unique structural units of O-antigens. Ultracentrifugation analysis revealed that tachylectin-3 is present in dimer in solution. A cDNA coding for tachylectin-3 was isolated from a hemocyte cDNA library. Tachylectin-3 consisted of two repeating sequences, each with a partial sequence similarity to rinderpest virus neuraminidase. Tachylectin-3 and three previously isolated types of tachylectins were all predominantly expressed in hemocytes and released from hemocytes in response to external stimuli. These lectins present at injured sites suggest that they probably serve synergistically to accomplish an effective host defense against invading microbes.

  antigen, lipopolysaccharides, O-antigen, specificity, blood group A, lectin

  NCBI PubMed ID: 9920866
  Publication DOI: 10.1074/jbc.274.6.3272
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: skawascb@mbox.nc.kyushu-u.ac.jp
  Institutions: Departments of Molecular Biology, Graduate School of Medical Science and Biology, Faculty of Science, Kyushu University, Fukuoka 812-8581, Department of Life Science, Faculty of Bioscience and Bioengineering, Tokyo Institute of Technology, Yokohama 226-8501, Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Tokyo 101-0062, Japan., Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, Tokyo 101-0062, Japan
  
   
  
  Escherichia coli O128
  CSDB ID 7240 (all data & tools)
• Article ID: 371
  Sengupta P, Bhattacharyya T, Majumder M, Chatterjee BP "Determination of the immunodominant part in the O-antigenic polysaccharide from Escherichia coli O128 by ELISA-inhibition study" - FEMS Immunology and Medical Microbiology 28(2) (2000) 133-137
  

  The immunodominant part in the O-antigenic polysaccharide from Escherichia coli O128 was immunologically characterized by an enzyme‐linked immunosorbent assay (ELISA). The antibody specificity was determined by the inhibitory effects of the methyl glycosides of constituent mono‐ and oligosaccharides synthesized related to the O-antigenic polysaccharide from E. coli O128. It was found that methyl α-L-fucopyranoside was the most effective inhibitor amongst the monosaccharides while the highest antibody specificity was directed towards the trisaccharide with the structure: β-D-GalpNAc-(1→6)-[α-L-Fuc-(1→2)-β-D-Galp-1→OMe suggesting that the monospecific antibody has the extended combining site.

  Lipopolysaccharide, O-antigenic polysaccharide, Escherichia coli O128, immunodominant, monospecific IgG

  NCBI PubMed ID: 10799803
  Publication DOI: 10.1111/j.1574-695X.2000.tb01467.x
  Journal NLM ID: 9315554
  Publisher: Elsevier
  Correspondence: bcbpc@mahendra.iacs.res.in
  Institutions: Department of Biological Chemistry, Indian Association for the Cultivation of Sciences, Calcutta, India
  Methods: immunochemical methods
  
   
  
  Escherichia coli O128
  CSDB ID 8302 (all data & tools)
• Article ID: 1200
  Sengupta P, Bhattacharyya T, Shashkov AS, Kochanowski H, Basu S "Structure of the O-specific side chain of the Escherichia coli O128 lipopolysaccharide" - Carbohydrate Research 277 (1995) 283-290
  

  Lipopolysaccharide, NMR, LPS, structure, chain, side chain, Escherichia, Escherichia coli, O-specific, Escherichia coli O128

  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Biological Chemistry, Indian Association for the Cultivation of Sciences, Calcutta, India
  Methods: NMR
  
   
  
  Escherichia coli O128
  CSDB ID 4646 (all data & tools)
• Article ID: 3196
  Stenutz R, Weintraub A, Widmalm G "The structures of Escherichia coli O-polysaccharide antigens" - FEMS Microbiology Reviews 30(3) (2006) 382-403
  

  Escherichia coli is usually a non-pathogenic member of the human colonic flora. However, certain strains have acquired virulence factors and may cause a variety of infections in humans and in animals. There are three clinical syndromes caused by E. coli: (i) sepsis/meningitis; (ii) urinary tract infection and (iii) diarrhoea. Furthermore the E. coli causing diarrhoea is divided into different 'pathotypes' depending on the type of disease, i.e. (i) enterotoxigenic; (ii) enteropathogenic; (iii) enteroinvasive; (iv) enterohaemorrhagic; (v) enteroaggregative and (vi) diffusely adherent. The serotyping of E. coli based on the somatic (O), flagellar (H) and capsular polysaccharide antigens (K) is used in epidemiology. The different antigens may be unique for a particular serogroup or antigenic determinants may be shared, resulting in cross-reactions with other serogroups of E. coli or even with other members of the family Enterobacteriacea. To establish the uniqueness of a particular serogroup or to identify the presence of common epitopes, a database of the structures of O-antigenic polysaccharides has been created. The E. coli database (ECODAB) contains structures, nuclear magnetic resonance chemical shifts and to some extent cross-reactivity relationships. All fields are searchable. A ranking is produced based on similarity, which facilitates rapid identification of strains that are difficult to serotype (if known) based on classical agglutinating methods. In addition, results pertinent to the biosynthesis of the repeating units of O-antigens are discussed. The ECODAB is accessible to the scientific community at http://www.casper.organ.su.se/ECODAB/

  NMR, structure, serotype, O-antigen, Enterobacteriacea, database

  NCBI PubMed ID: 16594963
  Publication DOI: 10.1111/j.1574-6976.2006.00016.x
  Journal NLM ID: 8902526
  Publisher: Oxford University Press
  Correspondence: andrej.weintraub@ki.se
  Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden
  
   
  
  Escherichia coli O128
  CSDB ID 20681 (all data & tools)
• Article ID: 3430
  Ali T, Weintraub A, Widmalm G "Structural studies of the O-antigenic polysaccharides from the enteroaggregative Escherichia coli strain 87/D2 and international type strains from E. coli O128" - Carbohydrate Research 343(4) (2008) 695-702
  

  The O-antigen of the lipopolysaccharide (LPS) from the enteroaggregative Escherichia coli strain 87/D2 has been determined by component analysis together with NMR spectroscopy. The polysaccharide has pentasaccharide repeating units in which all the residues have the galacto-configuration. The repeating unit of the O-antigen, elucidated using the O-deacylated LPS, is branched with the following structure: Analysis of the (1)H NMR spectrum of the LPS revealed O-acetyl groups (approximately 0.7 per repeating unit) distributed over two positions. Subsequent analysis showed that the galactose residue carries acetyl groups at either O-3 or O-4 in a ratio of approximately 2:1. The international reference strain from E. coli O128ab was investigated and the repeating unit of the O-antigens has the following structure: Analysis of the (1)H NMR spectrum of the LPS revealed O-acetyl groups (approximately one per repeating unit) distributed over two positions. The integrals of the resonances for the O-acetyl groups indicated similarities between the O-antigen from E. coli O128ab and that of E. coli strain 87/D2, whereas the O-acetyl substitution pattern in the E. coli O128ac O-antigen differed slightly. Enzyme immunoassay using specific anti-E. coli O128ab and anti-E. coli O128ac rabbit sera confirmed the results

  Lipopolysaccharide, NMR, Escherichia coli, serology, biological repeating unit, Enteroaggregative

  NCBI PubMed ID: 18237721
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: G. Widmalm
  Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden, Karolinska Institute, Department of Laboratory Medicine, Division of Clinical Microbiology, Karolinska University Hospital, Stockholm, Sweden
  Methods: 13C NMR, 1H NMR, NMR-2D, sugar analysis, GLC, mild acid hydrolysis, alkaline degradation, NMR-1D, immunochemical methods
  
   
  
  Escherichia coli O128ab
  CSDB ID 22801 (all data & tools)
• Article ID: 3503
  Li M, Liu XW, Shao J, Shen J, Jia Q, Yi W, Song JK, Woodward R, Chow CS, Wang PG "Characterization of a Novel a1,2-Fucosyltransferase of Escherichia coli O128:B12 and Functional Investigation of Its Common Motif" - Biochemistry 47(1) (2008) 378-387
  

  The wbsJ gene from Escherichia coli O128:B12 encodes an α1,2-fucosyltransferase responsible for adding a fucose onto the galactose residue of the O-antigen repeating unit via an α1,2 linkage. The wbsJ gene was overexpressed in E. coli BL21 (DE3) as a fusion protein with glutathione S-transferase (GST) at its N-terminus. GST-WbsJ fusion protein was purified to homogeneity via GST affinity chromatography followed by size exclusion chromatography. The enzyme showed broad acceptor specificity with Galβ1,3GalNAc (T antigen), Galβ1,4Man and Galβ1,4Glc (lactose) being better acceptors than Galβ-O-Me and galactose. Galβ1,4Fru (lactulose), a natural sugar, was furthermore found to be the best acceptor for GST-WbsJ with a reaction rate four times faster than that of lactose. Kinetic studies showed that GST-WbsJ has a higher affinity for lactose than lactulose with apparent Km values of 7.81 mM and 13.26 mM, respectively. However, the kcat/appKm value of lactose (6.36 M-1.min-1) is two times lower than that of lactulose (13.39 M-1.min-1). In addition, the α1,2-fucosyltransferase activity of GST-WbsJ was found to be independent of divalent metal ions such as Mn2+ or Mg2+. This activity was competitively inhibited by GDP with a Ki value of 1.41 mM. Site-directed mutagenesis and a GDP-bead binding assay were also performed to investigate the functions of the highly conserved motif H152xR154R155xD157. In contrast to α1,6-fucosyltransferases, none of the mutants of WbsJ within this motif exhibited a complete loss of enzyme activity. However, residues R154 and D157 were found to play critical roles in donor binding and enzyme activity. The results suggest that the common motif shared by both α1,2-fucosyltransferases and α1,6-fucosyltransferases have similar functions. Enzymatic synthesis of fucosylated sugars in milligram scale was successfully performed using Galβ-O-Me and Galβ1,4Glcβ-N3 as acceptors

  O-antigen, Escherichia coli, enzymatic synthesis, a-1, 2-fucosyltransferase, wbsJ gene

  NCBI PubMed ID: 18078329
  Journal NLM ID: 0370623
  Publisher: American Chemical Society
  Correspondence: wang.892@osu.edu
  Institutions: Department of Chemistry, Wayne State University, Detroit, Michigan 48202, and Department of Biochemistry and Chemistry, The Ohio State University, Columbus, Ohio 43210
  Methods: 13C NMR, 1H NMR, ESI-MS, NMR-1D, genetic methods, biochemical methods
  
   
  
  Escherichia coli O128:B12
  CSDB ID 22685 (all data & tools)
• Article ID: 5472
  Liu B, Furevi A, Perepelov AV, Guo X, Cao H, Wang Q, Reeves PR, Knirel YA, Wang L, Widmalm G "Structure and genetics of Escherichia coli O antigens" - FEMS Microbiology Reviews 44(6) (2020) 655-683
  

  Escherichia coli includes clonal groups of both commensal and pathogenic strains, with some of the latter causing serious infectious diseases. O antigen variation is current standard in defining strains for taxonomy and epidemiology, providing the basis for many serotyping schemes for Gram-negative bacteria. This review covers the diversity in E. coli O antigen structures and gene clusters, and the genetic basis for the structural diversity. Of the 187 formally defined O antigens, six (O31, O47, O67, O72, O94 and O122) have since been removed and four (O14, O34, O89 and O144) strains do not produce any O antigen. Therefore, structures are presented for 176 of the 181 E. coli O antigens, some of which include subgroups. Most (93%) of these O antigens are synthesized via the Wzx/Wzy pathway, 11 via the ABC transporter pathway, with O20, O57 and O60 still uncharacterized due to failure to find their O antigen gene clusters. Biosynthetic pathways are given for 38 of the 49 sugars found in E. coli O antigens, and several pairs or groups of the E. coli antigens that have related structures show close relationships of the O antigen gene clusters within clades, thereby highlighting the genetic basis of the evolution of diversity.

  structure, O antigen, Escherichia coli, gene cluster, serogroup, diversity

  NCBI PubMed ID: 31778182
  Publication DOI: 10.1093/femsre/fuz028
  Journal NLM ID: 8902526
  Publisher: Oxford University Press
  Correspondence: G. Widmalm ; Lei Wang
  Institutions: Department of Organic Chemistry, Arrhenius Laboratory, Stockholm University, Stockholm, Sweden, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Tianjin Key Laboratory of Microbial Functional Genomics, Tianjin, China, The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, Tianjin, China, School of Molecular and Microbial Bioscience (G08), University of Sydney, Sydney, Australia, TEDA Institute of Biological Sciences and Biotechnology, Nankai University, TEDA, Tianjin, China, Department of Immunology, School of Basic Medical Sciences, Tianjin Medical University, Tianjin, China
  
   
  
  Escherichia coli O128ab, Escherichia coli O128ac
  CSDB ID 1867 (all data & tools)