Show legend Show as text

Structure type: oligomer
Aglycon: (CH2)8CO2CH3
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,SB_165,SB_166,SB_187,SB_195,SB_30,SB_40,SB_7,SB_87,SB_88

• Article ID: 16
  Blixt O, Van Die I, Norberg T, van den Eijnden DH "High-level expression of the Neisseria meningitidis lgtA gene in Escherichia coli and characterization of the encoded N-acetylglucosaminyltransferase as a useful catalyst in the synthesis of GlcNAcb1→3Gal and GalNAcb1-3Gal linkages" - Glycobiology 9(10) (1999) 1061-1071
  

  We have expressed the Neisseria meningitidis lgtA gene at a high level in Escherichia coli. The encoded β-N-acetylglucosaminyltransferase, referred to as LgtA, which in the bacterium is involved in the synthesis of the lacto-N-neo-tetraose structural element of the bacterial lipooligosaccharide, was obtained in an enzymatically highly active form. This glycosyltransferase appeared to be unusual in that it displays a broad acceptor specificity toward both α- and β-galactosides, whether structurally related to N- or O-protein-, or lipid-linked oligosaccharides. Product analysis by one- and two-dimensional 400 MHz 1H- and 13C NMR spectroscopy reveals that LgtA catalyzes the introduction of GlcNAc from UDP-GlcNAc in a β1→3-linkage to accepting Gal residues. The enzyme can thus be characterized as a UDP-GlcNAc:Gal α/β-R β 3-N-acetylglucosaminyltransferase. Although lactose is a highly preferred acceptor substrate the recombinant enzyme also acts efficiently on monomeric and dimeric N-acetyllactosamine revealing its potential value in the synthesis of polylactosaminoglycan structures in enzyme assisted procedures. Furthermore, LgtA shows a high donor promiscuity toward UDP-GalNAc, but not toward other UDP-sugars, and can catalyze the introduction of GalNAc in β1→3-linkage to α- or β-Gal in the acceptor structures at moderate rates. LgtA therefore shows promise to be a useful catalyst in the preparative synthesis of both GlcNAc β1→3 Gal and GalNAc β1→3 Gal linkages.

  oligosaccharide, enzyme-assisted-synthesis, recombinant glycosyltransferase, glycosidic linkage, polylactosaminoglycan, recombinant glycosyltrasferase

  NCBI PubMed ID: 10521543
  Publication DOI: 10.1093/glycob/9.10.1061
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Department of Chemistry, Swedish University of Agricultural Sciences, Uppsala, Sweden, Department of Medical Chemistry, Vrije Universiteit, Van der Boechorstraat 7, 1081 BT Amsterdam, The Netherlands
  Methods: 13C NMR, 1H NMR, NMR-2D, SDS-PAGE, enzyme-assisted synthesis, DNA techniques, glycosyltransferase assays, kinetics assays
  
   
  
  Escherichia coli
  CSDB ID 1749 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 2 linear B blood-group determinant
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130650,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_40,SB_7,SB_87,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 F-15A
  CSDB ID 3540 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 2 linear B blood-group determinant
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130650,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_158538,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_40,SB_7,SB_87,SB_88

• Article ID: 1006
  Monteiro MA, Appelmelk BJ, Rasko DA, Moran AP, Hynes SO, MacLean LL, Chan KH, Michael FS, Logan SM, O'Rourke J, Lee A, Taylor DE, Perry MB "Lipopolysaccharide structures of Helicobacter pylori genomic strains 26695 and J99, mouse model H. pylori Sydney strain, H. pylori P466 carrying sialyl Lewis X, and H. pylori UA915 expressing Lewis B. Classification of H. pylori lipopolysaccharides into glycotype families" - European Journal of Biochemistry 267(2) (2000) 305-320
  

  This study describes the molecular makeup of the cell-wall lipopolysaccharides (LPSs) (O-chain polysaccharide→core oligosaccharide→lipid A) from five Helicobacter pylori strains: H. pylori 26695 and J99, the complete genome sequences of which have been published, the established mouse model Sydney strain (SS1), and the symptomatic strains P466 and UA915. All chemical and serological experiments were performed on the intact LPSs. H. pylori 26695 and SS1 possessed either a low-Mr semi-rough-form LPS carrying mostly a single Ley type-2 blood-group determinant in the O-chain region covalently attached to the core oligosaccharide or a high-Mr smooth-form LPS, as did strain J99, with an elongated partially fucosylated type-2 N-acetyllactosamine (polyLacNAc) O-chain polymer, terminated mainly by a Lex blood-group determinant, connected to the core oligosaccharide. In the midst of semi-rough-form LPS glycoforms, H. pylori 26695 and SS1 also expressed in the O-chain region a difucosylated antigen, α-L-Fucp(1-3)-α-L-Fucp(1-4)-β-D-GlcpNAc, and the cancer-cell-related type-1 or type-2 linear B-blood-group antigen, α-D-Galp(1-3)-β-D-Galp(1-3 or 4)-β-D-GlcpNAc. The LPS of H. pylori strain P466 carried the cancer-associated type-2 sialyl Lex blood-group antigen, and the LPS from strain UA915 expressed a type-1 Leb blood-group unit. These findings should aid investigations that focus on identifying and characterizing genes responsible for LPS biosynthesis in genomic strains 26695 and J99, and in understanding the role of H. pylori LPS in animal model studies. The LPSs from the H. pylori strains studied to date were grouped into specific glycotype families.

  Lipopolysaccharide, structure, Helicobacter pylori, Lewis x, histo-blood groups, glycotypes

  NCBI PubMed ID: 10632700
  Publication DOI: 10.1046/j.1432-1327.2000.01007.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: Mario.Monteiro@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori 26695
  CSDB ID 3577 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: lipid A
Trivial name: type 2 linear B blood-group determinant
Contained glycoepitopes: IEDB_115013,IEDB_120354,IEDB_123890,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130650,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140088,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189046,IEDB_2189047,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_30,SB_40,SB_7,SB_87,SB_88

• Article ID: 1006
  Monteiro MA, Appelmelk BJ, Rasko DA, Moran AP, Hynes SO, MacLean LL, Chan KH, Michael FS, Logan SM, O'Rourke J, Lee A, Taylor DE, Perry MB "Lipopolysaccharide structures of Helicobacter pylori genomic strains 26695 and J99, mouse model H. pylori Sydney strain, H. pylori P466 carrying sialyl Lewis X, and H. pylori UA915 expressing Lewis B. Classification of H. pylori lipopolysaccharides into glycotype families" - European Journal of Biochemistry 267(2) (2000) 305-320
  

  This study describes the molecular makeup of the cell-wall lipopolysaccharides (LPSs) (O-chain polysaccharide→core oligosaccharide→lipid A) from five Helicobacter pylori strains: H. pylori 26695 and J99, the complete genome sequences of which have been published, the established mouse model Sydney strain (SS1), and the symptomatic strains P466 and UA915. All chemical and serological experiments were performed on the intact LPSs. H. pylori 26695 and SS1 possessed either a low-Mr semi-rough-form LPS carrying mostly a single Ley type-2 blood-group determinant in the O-chain region covalently attached to the core oligosaccharide or a high-Mr smooth-form LPS, as did strain J99, with an elongated partially fucosylated type-2 N-acetyllactosamine (polyLacNAc) O-chain polymer, terminated mainly by a Lex blood-group determinant, connected to the core oligosaccharide. In the midst of semi-rough-form LPS glycoforms, H. pylori 26695 and SS1 also expressed in the O-chain region a difucosylated antigen, α-L-Fucp(1-3)-α-L-Fucp(1-4)-β-D-GlcpNAc, and the cancer-cell-related type-1 or type-2 linear B-blood-group antigen, α-D-Galp(1-3)-β-D-Galp(1-3 or 4)-β-D-GlcpNAc. The LPS of H. pylori strain P466 carried the cancer-associated type-2 sialyl Lex blood-group antigen, and the LPS from strain UA915 expressed a type-1 Leb blood-group unit. These findings should aid investigations that focus on identifying and characterizing genes responsible for LPS biosynthesis in genomic strains 26695 and J99, and in understanding the role of H. pylori LPS in animal model studies. The LPSs from the H. pylori strains studied to date were grouped into specific glycotype families.

  Lipopolysaccharide, structure, Helicobacter pylori, Lewis x, histo-blood groups, glycotypes

  NCBI PubMed ID: 10632700
  Publication DOI: 10.1046/j.1432-1327.2000.01007.x
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: Mario.Monteiro@nrc.ca
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario, Canada
  Methods: FAB-MS, NMR
  
   
  
  Helicobacter pylori Sydney
  CSDB ID 3624 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,SB_165,SB_166,SB_187,SB_195,SB_30,SB_40,SB_7,SB_87,SB_88

• Article ID: 2333
  Price SB, Phelps CJ, Wilkins TD, Johnson JL "Cloning of the carbohydrate-binding portion of the toxin A gene of Clostridium difficile" - Current Microbiology 16 (1987) 55-60
  
  Journal NLM ID: 7808448
  Publisher: Springer International
  
   
  
  Clostridium difficile
  CSDB ID 121722 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: oligosaccharide type 2 chains of B-2 antigen
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_140125,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144562,IEDB_146694,IEDB_149555,IEDB_149558,IEDB_150948,IEDB_150953,IEDB_151528,IEDB_151531,IEDB_152212,IEDB_152214,IEDB_153195,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_418918,IEDB_461716,IEDB_461719,IEDB_689191,IEDB_918314,SB_148,SB_154,SB_165,SB_166,SB_187,SB_195,SB_30,SB_34,SB_40,SB_7,SB_86,SB_87,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 25770 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_146694,IEDB_149144,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29495 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29496 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29497 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_146694,IEDB_149144,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29498 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_146694,IEDB_149144,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29499 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29500 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29501 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_146664,IEDB_146694,IEDB_149144,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR28
  CSDB ID 29502 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_115013,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130697,IEDB_135813,IEDB_135815,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_140108,IEDB_140109,IEDB_140110,IEDB_140122,IEDB_141496,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_153197,IEDB_190606,IEDB_418918,IEDB_689191,IEDB_918314,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_40,SB_6,SB_7,SB_87,SB_88

• Article ID: 4518
  Gebus C, Cottin C, Randriantsoa M, Drouillard S, Samain E "Synthesis of a-galactosyl epitopes by metabolically engineered Escherichia coli" - Carbohydrate Research 361 (2012) 83-90
  

  The α-Gal epitope is a carbohydrate structure, Galα-3Galβ-4GlcNAc-R, expressed on glycoconjuguates in many mammals, but not in humans. Species that do not express this epitope have present in their serum large amounts of natural anti-Gal antibodies, which contribute to organ hyperacute rejection during xenotransplantation. We first describe the efficient conversion of lactose into isoglobotriaose (Galα-3Galβ-4Glc) using high cell density cultures of a genetically engineered Escherichia coli strain expressing the bovine gene for α-1,3-galactosyltransferase. Attempts to produce the Galili pentasaccharide (Galα-3Galβ-4GlcNAcβ-3Galβ-4Glc) by additionally expressing the Neisseria meningitis lgtA gene for β-1,3-N-acetylglucosaminyltransferase and the Helicobacter pylori gene for β-1,4-galactosyltransferase were unsuccessful and led to the formation of a series of long chain oligosaccharides formed by the repeated addition of the trisaccharide motif [Galβ-4GlcNAcβ-3Galα-3] onto a lacto-N-neotetraose primer. The replacement of LgtA by a more specific β-1,3-N-acetylglucosaminyltransferase from H. pylori, which was unable to glycosylate α-galactosides, prevented the formation of these unwanted compounds and allowed the successful formation of the Galili pentasaccharide and longer α-Gal epitopes.

  Escherichia coli, Oligosaccharides, fermentation, Metabolic engineering, α-Gal epitope, a-Gal epitope

  NCBI PubMed ID: 23000215
  Publication DOI: 10.1016/j.carres.2012.05.015
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: S. Drouillard sophie.drouillard@cermav.cnrs.fr
  Institutions: Centre de recherche sur Macromolecules Vegetales (CERMAV-CNRS), BP 53, F-38041 Grenoble Cedex 9, France
  Methods: 13C NMR, 1H NMR, TLC, ESI-MS, chemical methods, genetic methods
  
   
  
  Escherichia coli MR47
  CSDB ID 29505 (all data & tools)