Show legend Show as text

Structure type: oligomer
Aglycon: LPS
Trivial name: Lewis b
Contained glycoepitopes: IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 603
  Appelmelk BJ, Martino MC, Veenhof E, Monteiro MA, Maaskant JJ, Negrini R, Lindh F, Perry MB, del Guidice G, Vandenbroucke-Grauls CMJE "Phase variation in H type 1 and Lewis a epitopes of Helicobacter pylori lipopolysaccharide" - Infection and Immunity 68(10) (2000) 5928-5932
  

  Helicobacter pylori NCTC11637 lipopolysaccharide (LPS) expresses the human blood group antigens Lewis x (Lex), Ley, and H type I. In this report, we demonstrate that the H type I epitope displays high-frequency phase variation. One variant expressed Lex and Ley and no H type I as determined by serology; this switch was reversible. Insertional mutagenesis in NCTC11637 of JHP563 (a poly(C) tract containing an open reading frame homologous to glycosyltransferases) yielded a transformant with a serotype similar to the phase variant. Structural analysis of the NCTC11637 LPS confirmed the loss of the H type I epitope. Sequencing of JHP563 in strains NCTC11637, an H type I-negative variant, and an H type I-positive switchback variant showed a C14 (gene on), C13 (gene off), and C14 tract, respectively. Inactivation of strain G27, which expresses Lex, Ley, H type I, and Lea, yielded a transformant that expressed Lex and Ley. We conclude that JHP563 encodes a b3-galactosyltransferase involved in the biosynthesis of H type I and Lea and that phase variation in H type I is due to C-tract changes in this gene. A second H type I-negative variant (variant 3a) expressed Lex and Lea and had lost both H type I and Ley expression. Inactivation of HP093-HP094 resulted in a transformant expressing Lex and lacking Ley and H type I. Structural analysis of a mutant LPS confirmed the serological data. We conclude that the HP093-HP094 a2-fucosyltransferase (a2-Fuct) gene product is involved in the biosynthesis of both Ley and Lex. Finally, we inactivated HP0379 in strain 3a. The transformant had lost both Lex and Lea expression, which demonstrates that the HP0379 gene product is both an a3- and an a4-FucT. Our data provide understanding at the molecular level of how H. pylori is able to diversify in the host, a requirement likely essential for successful colonization and transmission.

  Lipopolysaccharide, Phase variation, gene, phase, tract, variation, epitope, type, epitopes, Helicobacter pylori, Helicobacter, change, Lewis, fucosyltransferase, Lewis a

  NCBI PubMed ID: 10992504
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: BJ.Appelmelk.mm@med.vu.nl
  Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, 1081 BT Amsterdam, The Netherlands, IRIS Research Center, Chiron SpA, Siena, Laboratory Unit, City Hospital, Brescia, Italy, National Research Council, Ottawa, Canada, Isosep, Tullinge, Sweden
  Methods: PCR, DNA sequencing, FAB-MS, ELISA, MAb studies, insertional mutagenesis
  
   
  
  Helicobacter pylori
  CSDB ID 287 (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
Aglycon: lipid A
Trivial name: type 1 Lewis B determinant
Contained glycoepitopes: IEDB_130650,IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_140088,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142488,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,IEDB_983931,SB_100,SB_137,SB_146,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 CA2, Helicobacter pylori H428, Helicobacter pylori H507
  CSDB ID 3550 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: acetylphenylenediamine-HSA
Trivial name: Lewis b antigen determinant
Compound class: neoglycoconjugate
Contained glycoepitopes: IEDB_117715,IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135511,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_1391966,IEDB_141499,IEDB_141794,IEDB_141807,IEDB_142076,IEDB_142078,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_142489,IEDB_143248,IEDB_143249,IEDB_143794,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_157001,IEDB_174333,IEDB_190606,IEDB_226432,IEDB_423095,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,IEDB_983931,SB_100,SB_137,SB_145,SB_146,SB_150,SB_153,SB_154,SB_155,SB_156,SB_160,SB_161,SB_165,SB_166,SB_173,SB_174,SB_187,SB_192,SB_195,SB_29,SB_6,SB_7,SB_86,SB_88

• Article ID: 1358
  Appelmelk BJ, Simoons-Smit I, Negrini R, Moran AP, Aspinall GO, Forte JG, de Vries T, Quan H, Verboom T, Maaskant JJ, Ghiara P, Kuipers EJ, Bloemena E, Tadema TM, Townsend RR, Tyagarajan K, Crothers JM, Monteiro MA, Savio A, De Graaf J "Potential role of molecular mimicry between Helicobacter pylori lipopolysaccharide and host Lewis blood group antigens in autoimmunity" - Infection and Immunity 64 (1996) 2031-2040
  

  Helicobacter pylori is involved in gastritis, gastric and duodenal ulcers, gastric adenocarcinoma, and mucosa-associated lymphoid tissue lymphoma. Earlier studies already suggested a role for autoimmune phenomena in H. pylori-linked disease. We now report that lipopolysaccharides (LPS) of H. pylori express Lewis y, Lewis x, and H type I blood group structures similar to those commonly occurring in gastric mucosa. Immunization of mice and rabbits with H. pylori cells or purified LPS induced an anti-Lewis x or y or anti-H type I response, yielding antibodies that bound human and murine gastric glandular tissue, granulocytes, adenocarcinoma, and mucosa-associated lymphoid tissue lymphoma cells. Experimental oral infections in mice or natural infection in humans yielded anti-Lewis antibodies also. The beta chain of gastric (H+,K+)-ATPase, the parietal cell proton pump involved in acid secretion, contained Lewis y epitopes; gastric mucin contained Lewis x and y antigenic determinants. Growth in mice of a hybridoma that secretes H. pylori-induced anti-Lewis y monoclonal antibodies resulted in histopathological evidence of gastritis, which indicates a direct pathogenic role for anti-Lewis antibodies. In conclusion, our observations demonstrate that molecular mimicry between H. pylori LPS and the host, based on Lewis antigens, and provide understanding of an autoimmune mechanism for H. pylori-associated type B gastritis.

  Lipopolysaccharide, antigen, LPS, potential, molecular mimicry, Helicobacter pylori, S-type LPS, Lewis x, blood group antigens

  NCBI PubMed ID: 8675304
  Journal NLM ID: 0246127
  Publisher: American Society for Microbiology
  Correspondence: BJ.Appelmelk.mm@med.vu.nl
  Institutions: Department of Medical Microbiology, Vrije Universiteit, Medical School, Amsterdam, The Netherlands
  
   
  
  Helicobacter pylori
  CSDB ID 6364 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_130659,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22649 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_130659,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22951 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22954 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3471
  Gargiulo V, Garozzo D, Lanzetta R, Molinaro A, Sturiale L, De Castro C, Parrilli M "Rhizobium rubi(T): A Gram-Negative Phytopathogenic Bacterium Expressing the Lewis B Epitope on the Outer Core of its Lipooligosaccharide Fraction" - Chembiochem: a European Journal of Chemical Biology 9(11) (2008) 1830-1835
  

  The structure of the core oligosaccharide from the phytopathogenic bacterium Rhizobium rubi was deduced by combining information from complementary chemical approaches (alkaline and acid hydrolysis), similar to the 'overlap peptide' strategy. This structure is new and it contains two main oligosaccharide backbones that differ in the substitution degree of the external Kdo unit. The relevant feature shared by both oligosaccharides is the presence of a tetrasaccharide motif that is similar to the blood group Lewis B antigen (Le(B)). This epitope differs from Le(B) in the glycosidic configuration of the glucosamine unit (alpha and not beta) and in the occurrence of acetyls substituents at O3 and/or O4 of the galactose moiety. Other notable structural features are the location of the Dha residue, the presence of a α-glucose unit that is linked to the inner Kdo unit, the high number of acid sugars and the highly branched core structure

  structure, Lipooligosaccharide, epitope, core oligosaccharide, Phytopathogenic bacteria, Lewis B antigen, Rhizobium rubi

  NCBI PubMed ID: 18574826
  Publication DOI: 10.1002/cbic.200800191
  Journal NLM ID: 100937360
  Publisher: Weinheim, Germany: Wiley Interscience
  Correspondence: decastro@unina.it
  Institutions: Department of Organic Chemistry and Biochemistry, University of Napoli 'Federico II', Via Cintia 4, 80126 Napoli (Italy), Fax: (+39) 81674393
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, 31P NMR, acid hydrolysis, alkaline degradation, MALDI-MS, composition analysis
  
   
  
  Rhizobium rubi T
  CSDB ID 22955 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: oligosaccharide type 1 chains of antigen
Contained glycoepitopes: IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,SB_100,SB_137,SB_146,SB_154,SB_155,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 23167 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: oligosaccharide type 1 chains of Le(b) antigen
Contained glycoepitopes: IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,SB_100,SB_137,SB_146,SB_154,SB_155,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 25764 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_115136,IEDB_130650,IEDB_130659,IEDB_131182,IEDB_136044,IEDB_136045,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_141806,IEDB_141807,IEDB_142488,IEDB_142489,IEDB_144562,IEDB_144998,IEDB_146664,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423153,IEDB_461719,IEDB_983931,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_192,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 3945
  Silipo A, Molinaro A "The Diversity of the Core Oligosaccharide in Lipopolysaccharides" - Book: Endotoxins: Structure, Function and Recognition (series: Subcellular Biochemistry, Part 1) (2010) Vol. 53, Chapter 4, 69-99
  

  Bacterial lipopolysaccharides (LPSs) are the major component of the outer membrane of Gram-negative bacteria. They have a structural role since they contribute to the cellular rigidity by increasing the strength of cell wall and mediating contacts with the external environment that can induce structural changes to allow life in different conditions. Furthermore, the low permeability of the outer membrane acts as a barrier to protect bacteria from host-derived antimicrobial compounds. Lipopolysaccharides are amphiphilic macromolecules generally comprising three defined regions distinguished by their genetics, structures and function: the lipid A, the core oligosaccharide and a polysaccharide portion, the O-chain. In some Gram-negative bacteria LPS can terminate with the core portion to form rough type LPS (R-LPS, LOS). The core oligosaccharide is an often branched and phosphorylated heterooligosaccharide with less than fifteen sugars, more conserved in the inner region, proximal to the lipid A, and often carrying non-stoichiometric substitutions leading to variation and micro-heterogeneity. The core oligosaccharide contributes to the bacterial viability and stability of the outer membrane, can assure the serological specificity and possesses antigenic properties.

  core oligosaccharide, endotoxin, Gram-negative bacteria, innate immunity, glyco-conjugates

  NCBI PubMed ID: 20593263
  Publication DOI: 10.1007/978-90-481-9078-2_4
  Publisher: Springer Science+Business Media B.V.
  Correspondence: molinaro@unina.it
  Editors: Wang X, Quinn PJ
  Institutions: Dipartimento di Chimica Organica e Biochimica, Università di Napoli Federico II, Complesso Universitario Monte Santangelo, Via Cintia 4, Napoli, I-80126, Italy
  
   
  
  Agrobacterium rubi T, Agrobacterium rubi DSM 6772
  CSDB ID 31105 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Trivial name: Lewis b
Contained glycoepitopes: IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,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
  
   
  
  Helicobacter pylori
  CSDB ID 30213 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: Lewis b antigen Le(b), Lewis b antigen, Lewis B antigen Le(b)
Contained glycoepitopes: IEDB_130652,IEDB_130653,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_1391962,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144562,IEDB_149554,IEDB_149556,IEDB_150899,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461723,IEDB_461724,SB_100,SB_137,SB_146,SB_154,SB_155,SB_165,SB_166,SB_187,SB_195,SB_29,SB_7,SB_86,SB_88

• Article ID: 5024
  Maldonado RF, Sá-Correia I, Valvano MA "Lipopolysaccharide modification in Gram-negative bacteria during chronic infection" - FEMS Microbiology Reviews 40(4) (2016) 480-493
  

  The Gram-negative bacterial lipopolysaccharide (LPS) is a major component of the outer membrane that plays a key role in host-pathogen interactions with the innate immune system. During infection, bacteria are exposed to a host environment that is typically dominated by inflammatory cells and soluble factors, including antibiotics, which provide cues about regulation of gene expression. Bacterial adaptive changes including modulation of LPS synthesis and structure are a conserved theme in infections, irrespective of the type or bacteria or the site of infection. In general, these changes result in immune system evasion, persisting inflammation and increased antimicrobial resistance. Here, we review the modifications of LPS structure and biosynthetic pathways that occur upon adaptation of model opportunistic pathogens (Pseudomonas aeruginosa, Burkholderia cepacia complex bacteria, Helicobacter pylori and Salmonella enterica) to chronic infection in respiratory and gastrointestinal sites. We also discuss the molecular mechanisms of these variations and their role in the host-pathogen interaction.

  O antigen, Pseudomonas aeruginosa, lipid A, Helicobacter pylori, cystic fibrosis, Burkholderia cenocepacia, adaptive mutation, gastric ulcer

  NCBI PubMed ID: 27075488
  Publication DOI: 10.1093/femsre/fuw007
  Journal NLM ID: 8902526
  Publisher: Oxford University Press
  Correspondence: m.valvano@qub.ac.uk
  Institutions: Institute for Bioengineering and Biosciences, Department of Bioengineering, Instituto Superior Tecnico, Universidade de Lisboa, Lisbon, Portugal, Department of Microbiology and Immunology, University of Western Ontario, London, ON, Canada, Centre for Infection and Immunity, Queen's University Belfast, Belfast, UK
  
   
  
  Helicobacter pylori
  CSDB ID 12180 (all data & tools)
• Article ID: 5826
  Perepelov AV, Senchenkova SN, Knirel YA "Variations in expression of terminal antigenic determinants and acquirement of glycosylation of the poly(N-acetyllactosamine)chain in the lipopolysaccharide of Helicobacter pylori upon colonization of rhesus monkeys" - Biochemistry (Moscow) 85(2) (2020) 234-240
  

  Helicobacter pylori is an important human pathogen that causes gastritis, gastric and duodenal ulcers, and gastric cancer. O-polysaccharides of H. pylori lipopolysaccharide (LPS) are composed of (β1→3)-poly(N-acetyllactosamine) (polyLacNAc) decorated with multiple α-L-fucose residues. In many strains, their terminal LacNAc units are mono- or di-fucosylated to mimic Lewis X (Lex) and/or Lewis Y (Ley) oligosaccharides. The studies in rhesus macaques as a model of human infection by H. pylori showed that this bacterium adapts to the host during colonization by expressing host Lewis antigens. Here, we characterized LPS from H. pylori strains used in the previous study, including the parental J166 strain and the three derivatives (98-149, 98-169, and 98-181) isolated from rhesus macaques after long-term colonization. Chemical and NMR spectroscopic analyses of the LPS showed that the parent strain expressed Lex, Ley, and H type 1 terminal oligosaccharide units. The daughter strains were similar to the parental one in the presence of the same LPS core and fucosylated polyLacNAc chain of the same length but differed in the terminal oligosaccharide units. These were Lex in the isolates 98-149 and 98-169, which corresponded to the Lea phenotype of the host animals, and Ley was found in the 98-181 isolate from the macaque characterized by the Leb phenotype. As Lea and Leb are isomers of Lex and Ley, respectively, the observed correlation confirmed adaptation of the expression of terminal oligosaccharide units in H. pylori strains to the properties of the host gastric mucosa. The 98-181 strain also acquired glucosylation of the polyLacNAc chain and was distinguished by a lower expression of fucosylated internal LacNAc units (internal Lex) as a result of decoration of polyLacNAc with β-glucopyranose, which may also play a role in the bacterial adaptation.

  Lipopolysaccharide, O-polysaccharide, Helicobacter pylori, glucosylation, bacterial adaptation, Lewis antigen expression, poly(N-acetyllactosamine), rhesus macaque

  NCBI PubMed ID: 32093599
  Publication DOI: 10.1134/S0006297920020108
  Journal NLM ID: 0376536
  Publisher: Nauka/Interperiodica
  Correspondence: andreivperepelov@gmail.com
  Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GLC-MS, sugar analysis, ESI-MS, Smith degradation, GPC, mild acid degradation
  
   
  
  Helicobacter pylori J166, Helicobacter pylori 98-149, Helicobacter pylori 98-169, Helicobacter pylori 98-181
  CSDB ID 5193 (all data & tools)
• Article ID: 6049
  Di Lorenzo F, Duda KA, Lanzetta R, Silipo A, De Castro C, Molinaro A "A Journey from Structure to Function of Bacterial Lipopolysaccharides" - Chemical Reviews (2021)
  

  Lipopolysaccharide (LPS) is a crucial constituent of the outer membrane of most Gram-negative bacteria, playing a fundamental role in the protection of bacteria from environmental stress factors, in drug resistance, in pathogenesis, and in symbiosis. During the last decades, LPS has been thoroughly dissected, and massive information on this fascinating biomolecule is now available. In this Review, we will give the reader a third millennium update of the current knowledge of LPS with key information on the inherent peculiar carbohydrate chemistry due to often puzzling sugar residues that are uniquely found on it. Then, we will drive the reader through the complex and multifarious immunological outcomes that any given LPS can raise, which is strictly dependent on its chemical structure. Further, we will argue about issues that still remain unresolved and that would represent the immediate future of LPS research. It is critical to address these points to complete our notions on LPS chemistry, functions, and roles, in turn leading to innovative ways to manipulate the processes involving such a still controversial and intriguing biomolecule.

  Lipopolysaccharide, LPS, structure, Pathogenesis, carbohydrate, function, gram negative bacteria

  NCBI PubMed ID: 34286971
  Publication DOI: 10.1021/acs.chemrev.0c01321
  Journal NLM ID: 2985134R
  Publisher: Chem Rev
  Correspondence: Antonio Molinaro
  Institutions: Department of Chemical Sciences, University of Naples Federico II, via Cinthia 4, 80126 Naples, Italy, Task Force on Microbiome Studies, University of Naples Federico II, Via Cinthia 4, 80126 Naples, Italy, Research Center Borstel Leibniz Lung Center, Parkallee 4a, 23845 Borstel, Germany, Department of Agricultural Sciences, University of Naples Federico II, Via Universita 96, 80055 Portici, Naples, Italy, Department of Chemistry, School of Science, Osaka University, 1-1 Osaka University Machikaneyama, Toyonaka, Osaka 560-0043, Japan
  
   
  
  Helicobacter pylori
  CSDB ID 7928 (all data & tools)
• Article ID: 12760
  Tang X, Wang P, Shen Y, Song X, Benghezal M, Marshall BJ, Tang H, Li H "Lipopolysaccharide O-antigen profiles of Helicobacter pylori strains from Southwest China" - BMC Microbiology 23(1) (2023) 360
  

  Background: Helicobacter pylori lipopolysaccharide (LPS) structures vary among strains of different geographic origin. The aim of this study was to characterize the LPS O-antigen profiles of H. pylori strains isolated from Southwest China, and to further analyze the association of Lewis antigen expression with clinical outcomes and antibiotic resistance. Results: A total of 71 H. pylori isolates from Southwest China were included for LPS profiling by silver staining and Western blotting after SDS-PAGE electrophoresis. We demonstrated that all the clinical isolates had the conserved lipid A and core-oligosaccharide, whereas the O-antigen domains varied significantly among the isolates. Compared with the common presence of the glucan/heptan moiety in LPS O-antigen structure of European strains, the clinical isolates in this study appeared to lack the glucan/heptan moiety. The expression frequency of Lex, Ley, Lea, and Leb was 66.2% (47/71), 84.5% (60/71), 56.3% (40/71), and 31.0% (22/71), respectively. In total, the expression of type II Lex and/or Ley was observed in 69 (97.2%) isolates, while type I Lea and/or Leb were expressed in 49 (69.0%) isolates. No association of Lewis antigen expression with clinical outcomes or with antibiotic resistance was observed. Conclusions: H. pylori strains from Southwest China tend to produce heptan-deficient LPS and are more likely to express type I Lewis antigens as compared with Western strains. This may suggest that H. pylori evolves to change its LPS structure for adaptation to different hosts.

  antibiotic resistance; Helicobacter pylori; heptan; Lewis antigen; lipopolysaccharide; O-antigen

  NCBI PubMed ID: 37993791
  Publication DOI: 10.1186/s12866-023-03116-0
  Journal NLM ID: 100966981
  Publisher: Biomed Central
  Correspondence: H. Tang ; H. Li
  Institutions: Helicobacter pylori Research Laboratory, School of Biomedical Sciences, Marshall Centre for Infectious Disease Research and Training, University of Western Australia, Nedlands, Australia, West China Marshall Research Center for Infectious Diseases, Center of Infectious Diseases, West China Hospital, Sichuan University, Chengdu, 610041, Sichuan, China, Division of Infectious Diseases, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, 610041, Sichuan, China, State Key Laboratory of Oral Diseases & National Center for Stomatology & National Clinical Research Center for Oral Diseases &, Department of Orthognathic and TMJ Surgery, West China Hospital of Stomatology, Sichuan University, Chengdu, 610041, Sichuan, China
  Methods: SDS-PAGE, Western blotting, statistical analysis, antibacterial assay
  
   
  
  Helicobacter pylori
  CSDB ID 26412 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Aglycon: core-Trio(GlcNAc-Fuc-Hep)
Trivial name: type 2 Le(x)-type 1 Le(b)
Compound class: LPS
Contained glycoepitopes: IEDB_130646,IEDB_130652,IEDB_130653,IEDB_130654,IEDB_130697,IEDB_131182,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137354,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_142489,IEDB_143794,IEDB_144556,IEDB_144562,IEDB_145669,IEDB_147455,IEDB_149554,IEDB_149556,IEDB_149557,IEDB_150092,IEDB_150899,IEDB_150939,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153529,IEDB_153553,IEDB_158533,IEDB_174333,IEDB_190606,IEDB_2151203,IEDB_2151204,IEDB_241103,IEDB_241107,IEDB_423096,IEDB_461709,IEDB_461719,IEDB_461720,IEDB_461723,IEDB_461724,IEDB_885811,IEDB_952752,SB_100,SB_137,SB_146,SB_154,SB_155,SB_157,SB_165,SB_166,SB_173,SB_187,SB_195,SB_29,SB_30,SB_7,SB_86,SB_88

• Article ID: 5179
  Li H, Tang H, Debowski AW, Stubbs KA, Marshall BJ, Benghezal M "Lipopolysaccharide Structural Differences between Western and Asian Helicobacter pylori Strains" - Toxins 10(9) (2018) 364
  

  Recent structural analysis of the lipopolysaccharide (LPS) isolated from Helicobacter pylori G27 wild-type and O-antigen ligase mutant resulted in the redefinition of the core-oligosaccharide and O-antigen domains. The short core-oligosaccharide (Glc-Gal-Hep-III-Hep-II-Hep-I-KDO) and its attached trisaccharide (Trio, GlcNAc-Fuc-Hep) appear to be highly conserved structures among H. pylori strains. The G27 LPS contains a linear glucan?heptan linker between the core-Trio and distal Lewis antigens. This linker domain was commonly identified in Western strains. In contrast, out of 12 partial LPS structures of Asian strains, none displayed the heptan moiety, despite the presence of Lewis antigens. This raises the question of how Lewis antigens are attached to the Trio, and whether the LPS structure of Asian strains contain another linker. Of note, a riban was identified as a linker in LPS of the mouse-adapted SS1 strain, suggesting that alternative linker structures can occur. In summary, additional full structural analyses of LPS in Asian strains are required to assess the presence or absence of an alternative linker in these strains. It will also be interesting to study the glucan-heptan linker moieties in pathogenesis as H. pylori infections in Asia are usually more symptomatic than the ones presented in the Western world.

  Lipopolysaccharide, structure, Helicobacter pylori

  NCBI PubMed ID: 30205541
  Publication DOI: 10.3390/toxins10090364
  Journal NLM ID: 101530765
  Publisher: Basel: MDPI
  Correspondence: H.T. ; M.B.
  Institutions: West China Marshall Research Center for Infectious Diseases, Center of Infectious Diseases, West China Hospital of Sichuan University, Chengdu 610041, China, Helicobacter pylori Research Laboratory, School of Biomedical Sciences, Marshall Centre for Infectious Disease Research and Training, University of Western Australia, Nedlands, WA 6009, Australia, School of Molecular Sciences, University of Western Australia, Crawley, WA 6009, Australia
  
   
  
  Helicobacter pylori H-428, Helicobacter pylori H-507, Helicobacter pylori CA2
  CSDB ID 12667 (all data & tools)