Show legend Show as text

Structure type: fragment of a bigger structure
Trivial name: monofucosyl A type 1 histo-blood group epitope
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130648,IEDB_130652,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_885822,SB_100,SB_137,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 99
  Therisod H, Monteiro MA, Perry MB, Caroff M "Helicobacter mustelae lipid A structure differs from that of Helicobacter pylori" - FEBS Letters 499(1-2) (2001) 1-5
  

  The lipid A structure of the Gram-negative bacterium Helicobacter mustelae, a ferret gastric pathogen responsible for the onset of gastric diseases in its host, was investigated. Two variant lipid A structures were found in the same strain. One structure contained a bisphosphorylated β-(1→6)-linked D-glucosamine backbone disaccharide with hydroxytetradecanoic acid in amide linkages. Unlike the structure described for the lipid A of the related human Helicobacter pylori gastric pathogen, which contains a C1 phosphate moiety, this lipid A presented phosphate groups at both the C1 and C4' positions, and contained no octadecanoyl fatty acid, which is present in H. pylori. The second lipid A structure had a different fatty acid composition in that 3-OH C(16) replaced most of the amide-linked 3-OH C(14).

  structure, lipid A, endotoxin, Helicobacter mustelae, Helicobacter pylori

  NCBI PubMed ID: 11418100
  Publication DOI: 10.1016/S0014-5793(01)02496-6
  Journal NLM ID: 0155157
  Publisher: Elsevier
  Correspondence: martine.caroff@bbmpc.u-psud.fr
  Institutions: Equipe Endotoxines, UMR 8619 du Centre National de la Recherche Scientifique, Biochimie, Université de Paris-Sud, Orsay, France, Institute for Biological Sciences, National Research Council of Canada, Ottawa, ON, Canada
  Methods: 13C NMR, 1H NMR, NMR-2D, GC-MS, de-O-acylation, TLC, 31P NMR, GC, MALDI-TOF MS, composition analysis, PD-MS, NMR-1D
  
   
  
  Helicobacter pylori, Helicobacter mustelae
  CSDB ID 5203 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipopolysacharide core
Trivial name: monofucosyl A type 1 histo-blood group epitope
Contained glycoepitopes: IEDB_130648,IEDB_130652,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_885822,SB_100,SB_137,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1003
  Monteiro MA, Zheng PY, Appelmelk BJ, Perry MB "The lipopolysaccharide of Helicobacter mustelae type strain ATCC43772 expresses the monofucosyl A type 1 histo-blood group epitope" - FEMS Microbiology Letters 154(1) (1997) 103-109
  

  Lipopolysaccharide, LPS, structure, strain, O-antigen, group, structural determination, epitope, type, molecular mimicry, Helicobacter mustelae, Helicobacter, blood group A

  Journal NLM ID: 7705721
  Publisher: Blackwell Publishing
  Correspondence: Mario.Monteiro@nrc.ca
  Institutions: Canadian Bacterial Diseases Network, Institute for Biological Sciences,National Research Council Canada,Ottawa,Canada
  Methods: NMR, MS
  
   
  
  Helicobacter mustelae
  CSDB ID 3476 (all data & tools)
• Article ID: 4690
  Knirel YA, Gabius H, Blixt O, Rapoport EM, Khasbiullina NR, Shilova NV, Bovin NV "Human tandem-repeat-type galectins bind bacterial non-bGal polysaccharides" - Glycoconjugate Journal 31(1) (2014) 7-12
  

  Galectins are multifunctional effectors, for example acting as regulators of cell growth via protein-glycan interactions. The observation of capacity to kill bacteria for two tandem-repeat-type galectins, which target histo-blood epitopes toward this end (Stowell et al. Nat. Med. 16:295-301, 2010), prompted us to establish an array with bacterial polysaccharides. We addressed the question whether sugar determinants other than ?-galactosides may be docking sites, using human galectins-4, -8, and -9. Positive controls with histo-blood group ABH-epitopes and the E. coli 086 polysaccharide ascertained the suitability of the set-up. Significant signal generation, depending on type of galectin and polysacchride, was obtained. Presence of cognate ?-galactoside-related epitopes within a polysaccharide chain or its branch will not automatically establish binding properties, and structural constellations lacking galactosides, like rhamnan, were found to be active. These data establish the array as valuable screening tool, giving direction to further functional and structural studies.

  glycan, Bacterial polysaccharide, ABO, galectin, printed glycan array, rhamnoside

  NCBI PubMed ID: 24065176
  Publication DOI: 10.1007/s10719-013-9497-3
  Journal NLM ID: 8603310
  WWW link: doi:10.1007/s10719-013-9497-3
  Publisher: Kluwer Academic Publishers
  Correspondence: bovin@carb.ibch.ru
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prosp., 47, Moscow, Russian Federation, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya 16/10
  Methods: GPC, mild acid degradation, binding assays
  
   
  
  Helicobacter mustelae ATCC43772
  CSDB ID 30082 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 1 monofucosyl A blood-group determinant
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130652,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140088,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_885822,IEDB_983931,SB_100,SB_137,SB_149,SB_154,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1005
  Monteiro MA, Zheng P, Ho B, Yokota S, Amano K, Pan Z, Berg DE, Chan KH, MacLean LL, Perry MB "Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from Asian hosts: the propensity to express type 1 blood-group antigens" - Glycobiology 10(7) (2000) 701-713
  

  Past studies have shown that the cell surface lipopolysaccharides (LPSs) of the ubiquitous human gastric pathogen Helicobacter pylori (a type 1 carcinogen) isolated from people residing in Europe and North America express predominantly type 2 Lewis x (Le(x)) and Le(y) epitopes and, infrequently, type 1 Le(a), Le(b), and Le(d) antigens. This production of Lewis blood-group structures by H. pylori LPSs, similar to those found in the surfaces of human gastric cells, allows the bacterium to mimic its human niche. In this study, LPSs of H.pylori strains extracted from patients living in China, Japan, and Singapore were chemically and serologically analyzed. When compared with Western H.pylori LPSs, these Asian strains showed a stronger tendency to produce type 1 blood groups. Of particular interest, and novel observations in H.pylori, the O-chain regions of strains F-58C and R-58A carried type 1 Le(a) without the presence of type 2 Le(x), strains R-7A and H607 were shown to have the capability of producing the type 1 blood group A antigen, and strains CA2, H507, and H428 expressed simultaneously the difucosyl isomeric antigens, type 1 Le(b) and type 2 Le(y). The apparent proclivity for the production of type 1 histo-blood group antigens in Asian H.pylori LPSs, as compared with Western strains, may be an adaptive evolutionary effect in that differences in the gastric cell surfaces of the respective hosts might be significantly dissimilar to select for the formation of different LPS structures on the resident H.pylori strain.

  lipopolysaccharides, structural determination, Helicobacter pylori, histo-blood groups

  NCBI PubMed ID: 10910974
  Publication DOI: 10.1093/glycob/10.7.701
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Canada, Department of Microbiology, National University of Singapore, Singapore, Central Research Laboratory, Akita University School of Medicine, Akita, Japan, Departments of Molecular Microbiology and Genetics, Washington University School of Medicine, St. Louis, MO 63130, USA
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori R-7A
  CSDB ID 3545 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 1 difucosyl A blood-group determinant
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136095,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140088,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_157005,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423096,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_461723,IEDB_461724,IEDB_885822,IEDB_983931,SB_100,SB_102,SB_137,SB_146,SB_149,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 1005
  Monteiro MA, Zheng P, Ho B, Yokota S, Amano K, Pan Z, Berg DE, Chan KH, MacLean LL, Perry MB "Expression of histo-blood group antigens by lipopolysaccharides of Helicobacter pylori strains from Asian hosts: the propensity to express type 1 blood-group antigens" - Glycobiology 10(7) (2000) 701-713
  

  Past studies have shown that the cell surface lipopolysaccharides (LPSs) of the ubiquitous human gastric pathogen Helicobacter pylori (a type 1 carcinogen) isolated from people residing in Europe and North America express predominantly type 2 Lewis x (Le(x)) and Le(y) epitopes and, infrequently, type 1 Le(a), Le(b), and Le(d) antigens. This production of Lewis blood-group structures by H. pylori LPSs, similar to those found in the surfaces of human gastric cells, allows the bacterium to mimic its human niche. In this study, LPSs of H.pylori strains extracted from patients living in China, Japan, and Singapore were chemically and serologically analyzed. When compared with Western H.pylori LPSs, these Asian strains showed a stronger tendency to produce type 1 blood groups. Of particular interest, and novel observations in H.pylori, the O-chain regions of strains F-58C and R-58A carried type 1 Le(a) without the presence of type 2 Le(x), strains R-7A and H607 were shown to have the capability of producing the type 1 blood group A antigen, and strains CA2, H507, and H428 expressed simultaneously the difucosyl isomeric antigens, type 1 Le(b) and type 2 Le(y). The apparent proclivity for the production of type 1 histo-blood group antigens in Asian H.pylori LPSs, as compared with Western strains, may be an adaptive evolutionary effect in that differences in the gastric cell surfaces of the respective hosts might be significantly dissimilar to select for the formation of different LPS structures on the resident H.pylori strain.

  lipopolysaccharides, structural determination, Helicobacter pylori, histo-blood groups

  NCBI PubMed ID: 10910974
  Publication DOI: 10.1093/glycob/10.7.701
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Canada, Department of Microbiology, National University of Singapore, Singapore, Central Research Laboratory, Akita University School of Medicine, Akita, Japan, Departments of Molecular Microbiology and Genetics, Washington University School of Medicine, St. Louis, MO 63130, USA
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori R-7A
  CSDB ID 3546 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_130648,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_145670,IEDB_146664,IEDB_150948,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153206,IEDB_153553,IEDB_153554,IEDB_153555,IEDB_156996,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_2151202,IEDB_461719,IEDB_885822,IEDB_983931,SB_149,SB_154,SB_165,SB_166,SB_187,SB_192,SB_195,SB_21,SB_6,SB_7,SB_86,SB_88

• Article ID: 2826
  Gaffar A, Gibbons RJ, Tylewksa S "Oral compositions containing oligosaccharide for inhibition of Streptococcus pyogenes adhesion on oral cells" - USA Patent Applications (1991) 1-5
  
   
  
  Streptococcus pyogenes
  CSDB ID 149573 (all data & tools)

Show legend Show as text

Structure type: 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_1391961,IEDB_1391963,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141814,IEDB_142489,IEDB_143260,IEDB_144562,IEDB_144990,IEDB_149570,IEDB_150766,IEDB_150948,IEDB_151528,IEDB_152213,IEDB_152214,IEDB_152215,IEDB_152218,IEDB_153205,IEDB_153222,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_241096,IEDB_461710,IEDB_461714,IEDB_461719,IEDB_885822,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_86,SB_88

• Article ID: 3199
  Yi W, Bystricky P, Yao Q, Guo H, Zhu L, Li H, Shen J, Li M, Ganguly S, Bush CA, Wang PG "Two different O-polysaccharides from Escherichia coli O86 are produced by different polymerization of the same O-repeating unit." - Carbohydrate Research 341 (2006) 100-108
  

  The structure of a new O-polysaccharide from Escherichia coli O86:K62:B7 was determined using NMR and methylation analysis. The structure is as follows: [carbohydrate: see text]. Comparison with the previously published structure from E. coli O86:K2:H2 revealed that the O-polysaccharides from these two E. coli O86 serotypes share the same branched pentasaccharide repeating unit. However, they differ in the anomeric configuration of the linkage, the linkage position, and the identity of the residue through which polymerization occurs. The immunochemical activity of these two forms of LPS toward anti-B antibody was studied and compared. The results showed that LPS from E. coli O86:K2:H2 strain possesses higher blood group B reactivity. The immunoreactivity difference was explained by modeling of the O-repeating unit tetrasaccharide fragments. This finding provides a good system for the further study of O-polysaccharide biosynthesis especially the repeating unit polymerization mechanism.

  Lipopolysaccharide, O-polysaccharide, molecular modeling, blood group antigens, polymerization, O-Repeating unit, Blood group antigens; Lipopolysaccharide; Molecular modeling; O-Polysaccharide; O-Repeating unit; Polymerization

  NCBI PubMed ID: 16313893
  Publication DOI: 10.1016/j.carres.2005.11.001
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: Peng G. Wang
  Institutions: Department of Biochemistry, The Ohio State University, Columbus, OH 43210, USA, Department of Chemistry, University of Maryland, Baltimore County, MD 21250, USA
  Methods: methylation, GC-MS, NMR, ELISA, composition analysis
  
   
  
  Escherichia coli O86:K61:B7
  CSDB ID 20618 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: oligosaccharide type 1 chains of antigen
Contained glycoepitopes: IEDB_130648,IEDB_130652,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_885822,SB_100,SB_137,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3520
  Moran AP "Relevance of fucosylation and Lewis antigen expression in the bacterial gastroduodenal pathogen Helicobacter pylori" - Carbohydrate Research 343(12) (2008) 1952-1965
  

  Helicobacter pylori is a prevalent bacterial, gastroduodenal pathogen of humans that can express Lewis (Le) and related antigens in the O-chains of its surface lipopolysaccharide. The O-chains of H. pylori are commonly composed of internal Le(x) units with terminal Le(x) or Le(y) units or, in some strains, with additional units of Le(a), Le(b), Le(c), sialyl-Le(x) and H-1 antigens, as well as blood groups A and B, thereby producing a mosaicism of antigenic units expressed. The genetic determination of the Le antigen biosynthetic pathways in H. pylori has been studied, and despite striking functional similarity, low sequence homology occurs between the bacterial and mammalian α(1,3/4)- and α(1,2)-fucosyltransferases. Factors affecting Le antigen expression in H. pylori, that can influence the biological impact of this molecular mimicry, include regulation of fucosyltransferase genes through slipped-strand mispairing, the activity and expression levels of the functional enzymes, the preferences of the expressed enzyme for distinctive acceptor molecules and the availability of activated sugar intermediates. Le mimicry was initially implicated in immune evasion and gastric adaptation by the bacterium, but more recent studies show a role in gastric colonization and bacterial adhesion with galectin-3 identified as the gastric receptor for polymeric Le(x) on the bacterium. From the host defence aspect, innate immune recognition of H. pylori by surfactant protein D is influenced by the extent of LPS fucosylation. Furthermore, Le antigen expression affects both the inflammatory response and T-cell polarization that develops after infection. Although controversial, evidence suggests that long-term H. pylori infection can induce autoreactive anti-Le antibodies cross-reacting with the gastric mucosa, in part leading to the development of gastric atrophy. Thus, Le antigen expression and fucosylation in H. pylori have multiple biological effects on pathogenesis and disease outcome.

  molecular mimicry, Helicobacter pylori, Fucosyltransferases, bacterial pathogenesis, Lewis antigens, fucosylation

  NCBI PubMed ID: 18279843
  Publication DOI: 10.1016/j.carres.2007.12.012
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: anthony.moran@nuigalway.ie
  Institutions: Department of Microbiology, School of Natural Sciences, National University of Ireland, Galway, Ireland, Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland 4222, Australia
  Methods: NMR, sugar analysis, MS, genetic methods
  
   
  
  Helicobacter pylori
  CSDB ID 23168 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: oligosaccharide type 2 chains of antigen
Contained glycoepitopes: IEDB_130646,IEDB_130648,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_140108,IEDB_140122,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144562,IEDB_149555,IEDB_149569,IEDB_150947,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153537,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_461713,IEDB_461719,IEDB_885822,SB_103,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_203,SB_30,SB_34,SB_7,SB_86,SB_88

• Article ID: 3520
  Moran AP "Relevance of fucosylation and Lewis antigen expression in the bacterial gastroduodenal pathogen Helicobacter pylori" - Carbohydrate Research 343(12) (2008) 1952-1965
  

  Helicobacter pylori is a prevalent bacterial, gastroduodenal pathogen of humans that can express Lewis (Le) and related antigens in the O-chains of its surface lipopolysaccharide. The O-chains of H. pylori are commonly composed of internal Le(x) units with terminal Le(x) or Le(y) units or, in some strains, with additional units of Le(a), Le(b), Le(c), sialyl-Le(x) and H-1 antigens, as well as blood groups A and B, thereby producing a mosaicism of antigenic units expressed. The genetic determination of the Le antigen biosynthetic pathways in H. pylori has been studied, and despite striking functional similarity, low sequence homology occurs between the bacterial and mammalian α(1,3/4)- and α(1,2)-fucosyltransferases. Factors affecting Le antigen expression in H. pylori, that can influence the biological impact of this molecular mimicry, include regulation of fucosyltransferase genes through slipped-strand mispairing, the activity and expression levels of the functional enzymes, the preferences of the expressed enzyme for distinctive acceptor molecules and the availability of activated sugar intermediates. Le mimicry was initially implicated in immune evasion and gastric adaptation by the bacterium, but more recent studies show a role in gastric colonization and bacterial adhesion with galectin-3 identified as the gastric receptor for polymeric Le(x) on the bacterium. From the host defence aspect, innate immune recognition of H. pylori by surfactant protein D is influenced by the extent of LPS fucosylation. Furthermore, Le antigen expression affects both the inflammatory response and T-cell polarization that develops after infection. Although controversial, evidence suggests that long-term H. pylori infection can induce autoreactive anti-Le antibodies cross-reacting with the gastric mucosa, in part leading to the development of gastric atrophy. Thus, Le antigen expression and fucosylation in H. pylori have multiple biological effects on pathogenesis and disease outcome.

  molecular mimicry, Helicobacter pylori, Fucosyltransferases, bacterial pathogenesis, Lewis antigens, fucosylation

  NCBI PubMed ID: 18279843
  Publication DOI: 10.1016/j.carres.2007.12.012
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: anthony.moran@nuigalway.ie
  Institutions: Department of Microbiology, School of Natural Sciences, National University of Ireland, Galway, Ireland, Institute for Glycomics, Gold Coast Campus, Griffith University, Queensland 4222, Australia
  Methods: NMR, sugar analysis, MS, genetic methods
  
   
  
  Helicobacter pylori
  CSDB ID 23174 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: oligosaccharide type 1 chains of A-1 antigen
Contained glycoepitopes: IEDB_130648,IEDB_130652,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391962,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149568,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153223,IEDB_153536,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_461709,IEDB_461712,IEDB_461719,IEDB_885822,SB_100,SB_137,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3903
  Moran A "The Role of Endotoxin in Infection: Helicobacter pylori and Campylobacter jejuni" - Book: Endotoxins: Structure, Function and Recognition (series: Subcellular Biochemistry, Part 1) (2010) Vol. 53, Chapter 10, 209-240
  

  Both Helicobacter pylori and Campylobacter jejuni are highly prevalent Gram-negative microaerophilic bacteria which are gastrointestinal pathogens of humans; H. pylori colonizes the gastroduodenal compartment and C. jejuni the intestinal mucosa. Although H. pylori causes chronic gastric infection leading to gastritis, peptic ulcers and eventually gastric cancer while C. jejuni causes acute infection inducing diarrhoeal disease, the endotoxin molecules of both bacterial species contrastingly contribute to their pathogenesis and the autoimmune sequelae each induces. Compared with enterobacterial endotoxin, that of H. pylori has significantly lower endotoxic and immuno-activities, the molecular basis for which is the underphosphorylation and underacylation of the lipid A component that interacts with immune receptors. This induction of low immunological responsiveness by endotoxin may aid the prolongation of H. pylori infection and therefore infection chronicity. On the other hand, this contrasts with acute infection-causing C. jejuni where overt inflammation contributes to pathology and diarrhoea production, and whose endotoxin is immunologically and endotoxically active. Futhermore, both H. pylori and C. jejuni exhibit molecular mimicry in the saccharide components of their endotoxins which can induce autoreactive antibodies; H. pylori expresses mimicry of Lewis and some ABO blood group antigens, C. jejuni mimicry of gangliosides. The former has been implicated in influencing the development of inflammation and gastric atrophy (a precursor of gastic cancer), the latter is central to the development of the neurological disorder Guillain-Barre syndrome. Both diseases raise important questions concerning infection-induced autoimmunity awaiting to be addressed.

  lipid A, Campylobacter jejuni, molecular mimicry, Helicobacter pylori, bacterial pathogenesis

  NCBI PubMed ID: 20593269
  Publication DOI: 10.1007/978-90-481-9078-2_10
  Publisher: Springer Science+Business Media B.V.
  Correspondence: anthony.moran@nuigalway.ie
  Editors: Wang X, Quinn PJ
  Institutions: Laboratory of Molecular Biochemistry, Microbiology, School of Natural Sciences, National University of Ireland, Galway, Ireland
  
   
  
  Helicobacter pylori
  CSDB ID 25765 (all data & tools)

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Structure type: fragment of a bigger structure
Trivial name: blood group A
Contained glycoepitopes: IEDB_130648,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_140124,IEDB_141584,IEDB_141794,IEDB_142489,IEDB_144562,IEDB_150948,IEDB_152213,IEDB_152214,IEDB_152218,IEDB_153205,IEDB_153553,IEDB_153554,IEDB_174039,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_885822,SB_149,SB_154,SB_165,SB_166,SB_187,SB_195,SB_7,SB_86,SB_88

• Article ID: 4666
  Brockhausen I "Crossroads between Bacterial and Mammalian Glycosyltransferases" - Frontiers in Immunology 5 (2014) 492
  

  Bacterial glycosyltransferases (GT) often synthesize the same glycan linkages as mammalian GT; yet, they usually have very little sequence identity. Nevertheless, enzymatic properties, folding, substrate specificities, and catalytic mechanisms of these enzyme proteins may have significant similarity. Thus, bacterial GT can be utilized for the enzymatic synthesis of both bacterial and mammalian types of complex glycan structures. A comparison is made here between mammalian and bacterial enzymes that synthesize epitopes found in mammalian glycoproteins, and those found in the O antigens of Gram-negative bacteria. These epitopes include Thomsen-Friedenreich (TF or T) antigen, blood group O, A, and B, type 1 and 2 chains, Lewis antigens, sialylated and fucosylated structures, and polysialic acids. Many different approaches can be taken to investigate the substrate binding and catalytic mechanisms of GT, including crystal structure analyses, mutations, comparison of amino acid sequences, NMR, and mass spectrometry. Knowledge of the protein structures and functions helps to design GT for specific glycan synthesis and to develop inhibitors. The goals are to develop new strategies to reduce bacterial virulence and to synthesize vaccines and other biologically active glycan structures.

  glycosyltransferases, protein structure, specificities, glycoprotein epitopes, glycan mimics

  Publication DOI: 10.3389/fimmu.2014.00492
  Journal NLM ID: 101560960
  Publisher: Lausanne: Frontiers Research Foundation
  Correspondence: brockhau@queensu.ca
  Institutions: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON, Canada, Department of Biomedical and Molecular Sciences, Queen's University, 18 Stuart Street, Kingston, ON K7L3N6
  
   
  
  Bacteroides ovatus
  CSDB ID 30217 (all data & tools)