Show legend Show as text

Structure type: suggested polymer biological repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130648,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_143794,IEDB_144990,IEDB_150899,IEDB_151528,IEDB_151531,IEDB_167071,IEDB_190606,SB_137,SB_156,SB_165,SB_166,SB_173,SB_187,SB_195,SB_29,SB_7,SB_88

• Article ID: 210
  Wang L, Huskic S, Cisterne A, Rothemund D, Reeves PR "The O-antigen gene cluster of Escherichia coli O55:H7 and identification of a new UDP-GlcNAc C4 epimerase gene" - Journal of Bacteriology 184(10) (2002) 2620-2625
  

  Escherichia coli O55 is an important antigen which is often associated with enteropathogenic E. coli clones. We sequenced the genes responsible for its synthesis and identified genes for O-antigen polymerase, O-antigen flippase, four enzymes involved in GDP-colitose synthesis, and three glycosyltransferases, all by comparison with known genes. Upstream of the normal O-antigen region there is a gne gene, which encodes a UDP-GlcNAc epimerase for converting UDP-GlcNAc to UDP- GalNAc and is essential for O55 antigen synthesis. The O55 gne product has only 20 and 26% identity to the gne genes of Pseudomonas aeruginosa and E. coli O113, respectively. We also found evidence for the O55 gene cluster's having evolved from another gene cluster by gain and loss of genes. Only three of the GDP-colitose pathway genes are in the usual location, the other two being separated, although nearby. It is thought that the E. coli O157:H7 clone evolved from the O55:H7 clone in part by transfer of the O157 gene cluster into an O55 lineage. Comparison of genes flanking the O-antigen gene clusters of the O55:H7 and O157:H7 clones revealed one recombination site within the galF gene and located the other between the hisG and amn genes. Genes outside the recombination sites are 99.6 to 100% identical in the two clones, while most genes thought to have transferred with the O157 gene cluster are 95 to 98% identical

  synthesis, transfer, antigen, gene, microbiology, O-antigen, O antigen, Pseudomonas, Pseudomonas aeruginosa, Escherichia, Escherichia coli, cluster, gene cluster, glycosyltransferases, identification, region, epimerase, enzyme, glycosyltransferase, site, Enzymes, clone, comparison, enteropathogenic, location, loss, O-antigen polymerase, O157, pathway, recombination

  NCBI PubMed ID: 11976290
  Journal NLM ID: 2985120R
  Publisher: American Society for Microbiology
  Correspondence: reeves@angis.org.au
  Institutions: Department of Microbiology, The University of Sydney, Sydney, New South Wales 2006, Australia
  Methods: genetic methods
  
   
  
  Escherichia coli O55
  CSDB ID 5554 (all data & tools)
• Article ID: 267
  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 O55
  CSDB ID 7239 (all data & tools)
• Article ID: 1778
  Knirel YA, Kochetkov NK "The structure of lipopolysaccharides of gram-negative bacteria. III. The structure of O-antigens: A review" - Biochemistry (Moscow) 59(12) (1994) 1325-1383
  

  This review summarizes data on the composition and structure of the O-antigens, the polysaccharide chains of the outer-membrane lipopolysaccharides (LPS) of Gram-negative bacteria defining the immunospecificity of these microbial cells. Special reference is given to some structural features of the O-antigens, such as the presence of unique monosaccharides and noncarbohydrate components, masked regularity, and the occurrence in one microorganism of LPS with structurally different polysaccharide chains. Antigenic relationships between microorganisms belonging to different taxonomic groups are discussed.

  structure, O-antigen, chemical composition, bacterial lipopolysaccharides, Salmonella livingstone C1

  NCBI PubMed ID: 7533007
  Journal NLM ID: 0376536
  Publisher: Nauka/Interperiodica
  Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
  
   
  
  Salmonella greenside Z, Escherichia coli O55
  CSDB ID 108629 (all data & tools)
• Article ID: 1989
  Lindberg B, Lindh F, Lönngren J, Lindberg AA, Svenson SB "Structural studies of the O-specific side-chain of the lipopolysaccharide from Escherichia coli O 55" - Carbohydrate Research 97(1) (1981) 105-112
  

  The structure of the O-specificside-chains of the lipopolysaccharide from Escherichiacoli O 55 has been investigated, methylation analysis, specific degradations, and n.m.r. spectroscopy being the principal methods used. It is concluded that the O-specificside-chains are composed of pentasaccharide repeating-units having the following structure [formula: see text, where Col stands for colitose (3,6-dideoxy-l-xylo-hexose)].

  Publication DOI: doi.org/10.1016/S0008-6215(00)80528-5
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Department of Organic Chemistry, Arrhenius Laboratory, University of Stockholm, Stockholm, Sweden
  Methods: 13C NMR, 1H NMR, methylation, GLC-MS, partial acid hydrolysis, sugar analysis, GLC, mild acid hydrolysis, Smith degradation, de-N-acetylation/deamination, oxidation with chromium trioxide
  
   
  
  Escherichia coli O55 (Su 3912/41)
  CSDB ID 113595 (all data & tools)
• Article ID: 3197
  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 O55
  CSDB ID 20658 (all data & tools)
• Article ID: 4318
  Huang JX, Azad MA, Yuriev E, Baker MA, Nation RL, Li J, Cooper MA, Velkov T "Molecular Characterization of Lipopolysaccharide Binding to Human a-1-Acid Glycoprotein" - Journal of Lipids 2012 (2012) 475153
  

  The ability of AGP to bind circulating lipopolysaccharide (LPS) in plasma is believed to help reduce the proinflammatory effect of bacterial lipid A molecules. Here, for the first time we have characterized human AGP binding characteristics of the LPS from a number of pathogenic Gram-negative bacteria: Escherichia coli, Salmonella typhimurium, Klebsiella pneumonia, Pseudomonas aeruginosa, and Serratia marcescens. The binding affinity and structure activity relationships (SAR) of the AGP-LPS interactions were characterized by surface plasma resonance (SPR). In order to dissect the contribution of the lipid A, core oligosaccharide and O-antigen polysaccharide components of LPS, the AGP binding affinity of LPS from smooth strains, were compared to lipid A, Kdo2-lipid A, R(a), R(d), and R(e) rough LPS mutants. The SAR analysis enabled by the binding data suggested that, in addition to the important role played by the lipid A and core components of LPS, it is predominately the unique species- and strain-specific carbohydrate structure of the O-antigen polysaccharide that largely determines the binding affinity for AGP. Together, these data are consistent with the role of AGP in the binding and transport of LPS in plasma during acute-phase inflammatory responses to invading Gram-negative bacteria.

  O-antigen, lipid A, gram negative bacteria, lipopolysaccharide-binding, AGP binding, SPR

  NCBI PubMed ID: 23316371
  Publication DOI: 10.1155/2012/475153
  Journal NLM ID: 101553819
  Publisher: Cairo: Hindawi Pub Corp
  Correspondence: Tony Velkov
  Institutions: Institute for Molecular Bioscience, The University of Queensland, 306 Carmody Road, St. Lucia, QLD 4072, Australia, Drug Development and Innovation, Drug Delivery, Disposition and Dynamics, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia, Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia, Priority Research Centre in Reproductive Science, School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia
  Methods: molecular modeling, fluorescence spectroscopy, surface plasmon resonance (SPR)
  
   
  
  Escherichia coli O55:B5
  CSDB ID 28398 (all data & tools)
• Article ID: 5183
  Ma Z, Zhang H, Li L, Chen M, Wang PG "Direct Cloning of Bacterial Surface Polysaccharide Gene Cluster for One-step Production of Glycoconjugate Vaccine" - ACS Infectious Diseases 5(1) (2019) 74-78
  

  Bacterial pathogen infections are fast-growing public health threats and worldwide problems. Glycoconjugate vaccines are among the most effective means in combating such infections. Recent advances in bacterial protein glycan coupling technology (PGCT) have revolutionized the production of glycoconjugate vaccines and drawn enormous attention from both researchers and pharmaceutical companies. Cloning of bacterial surface polysaccharide gene cluster is a prerequisite for the application of PGCT. In this study, we applied the RecET direct cloning strategy for rapid and efficient cloning of O-antigen polysaccharide gene clusters from Escherichia coli serotypes O25b, O26, and O55 in a high-fidelity manner. Then, these gene clusters were applied in PGCT to produce corresponding glycoconjugates. Subsequent immunological studies verified the abilities of glycoconjugate vaccine candidates O25-maltose-binding protein (MBP), O26-MBP, and O55-MBP to generate serotype-specific antibodies and confer protection against E. coli infections. The combination of RecET direct cloning and PGCT makes the rapid production of glycoconjugate vaccines against fast-expanding bacterial pathogens possible.

  glycoengineering, glycoconjugate vaccine, bacterial surface polysaccharide gene cluster, PGCT, RecET direct cloning

  NCBI PubMed ID: 30445812
  Publication DOI: 10.1021/acsinfecdis.8b00187
  Journal NLM ID: 101654580
  Publisher: Washington, DC: American Chemical Society
  Correspondence: pwang11@gsu.edu
  Institutions: Department of Chemistry, Georgia State University, 100 Piedmont Avenue, Atlanta, Georgia 30303, United States, National Glycoengineering Research Center, Shandong Provincial Key Laboratory of Carbohydrate Chemistry and Glycobiology, Shandong University, 27 ShanDa Nan Road, Jinan, Shandong 250100, China
  Methods: PCR, SDS-PAGE, DNA techniques, Western blotting, serum bactericidal assays, immunological assays, conjugation, RecET direct cloning
  
   
  
  Escherichia coli O55
  CSDB ID 12676 (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 O55
  CSDB ID 1562 (all data & tools)