Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 412
  Wang J, Villeneuve S, Zhang J, Lei PS, Miller CE, Lafaye P, Nato F, Szu SSC, Karpas A, Bystricky S, Robbins JB, Kovác P, Fournier JM, Glaudemans CPJ "On the antigenic determinants of the lipopolysaccharides of Vibrio cholerae O:1, serotypes Ogawa and Inaba" - Journal of Biological Chemistry 273(5) (1998) 2777-2783
  

  Monoclonal, murine IgG1s S-20-4, A-20-6, and IgA 2D6, directed against Vibrio cholerae O:1 Ogawa-lipopolysaccharide exhibited the same fine specificities and similar affinities for the synthetic methyl α-glycosides of the (oligo)saccharide fragments mimicking the Ogawa O-polysaccharide (O-PS). They did not react with the corresponding synthetic fragments of Inaba O-PS. IgG1s S-20-4 and A-20-6 have absolute affinity constants for synthetic Ogawa mono- to hexasaccharides of from approximately 10(5) to approximately 10(6) M-1. For IgG1s S-20-4, A-20-6, and IgA 2D6, the nonreducing terminal residue of Ogawa O-PS is the dominant determinant, accounting for approximately 90% of the maximal binding energy shown by these antibodies. Binding studies of derivatives of the Ogawa monosaccharide and IgGs S-20-4 and A-20-6 revealed that the C-2 O-methyl group fits into a somewhat flexible antibody cavity and that hydrogen bonds involving the oxygen and, respectively, the OH at the 2- and 3-position of the sugar moiety as well as the 2'-position in the amide side chain are required. Monoclonal IgA ZAC-3 and IgG3 I-24-2 are specific for V. cholerae O:1 serotypes Ogawa/Inaba-LPS.1 The former did not show binding with members of either series of the synthetic ligands related to the O-antigens of the Ogawa or Inaba serotypes, in agreement with its reported specificity for the lipid/core region (1). Inhibition studies revealed that the binding of purified IgG3 I-24-2 to Ogawa-LPS might be mediated by a region in the junction of the OPS to the lipid-core region of the LPS. cDNA cloning and analysis of the anti-Ogawa antibodies S-20-4, A-20-6, and 2D6 revealed a very high degree of homology among the heavy chains. Among the light chains, no such homology between S-20-4 and A-20-6 on the one hand, and 2D6 on the other hand, exists. For the anti-Inaba/Ogawa antibodies I-24-2 and ZAC-3, their heavy chains are completely different, with some homology among the light chains

  Lipopolysaccharide, lipopolysaccharides, LPS, serotype, antigenic, antigenic determinant, determinant, Serotypes, Vibrio, Vibrio cholerae

  NCBI PubMed ID: 9446585
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: glau@helix.nih.gov
  Institutions: Laboratory of Medicinal Chemistry, NIDDK and the Laboratory of Developmental and Molecular Immunity, NICHD, National Institutes of Health, Bethesda, MD, USA, Unite du Cholera et des Vibrions, Centre National de Reference des Vibrions et du Cholera and Hybridolab, Institut Pasteur, Paris, France
  Methods: 1H NMR, PCR, DNA sequencing, SDS-PAGE, ELISA, genetic methods
  
   
  
  Vibrio cholerae O1 Ogawa
  CSDB ID 8783 (all data & tools)
• Article ID: 1323
  Zhang J, Kovác P "Synthesis of methyl a-glycosides of some higher oligosaccharide fragments of the O-antigen of Vibrio cholerae O1, serotype Inaba and Ogawa" - Carbohydrate Research 300(4) (1997) 329-339
  

  The title oligosaccharides, the tri- through the hexasaccharide in the Inaba series and the penta- and the hexasaccharide in the Ogawa series, have been synthesized using 1-thioglycosides of precursors to 3-O-benzyl-perosamine (4-amino-4,6-dideoxy-D-mannose) as building blocks and N-iodosuccinimide/silver triflate as a promoter. The azido groups in the assembled oligosaccharides were reduced to amino groups, which were then acylated using 2,4-O-benzylidene-3-deoxy-L-glycero-tetronic acid as the derivatizing reagent. Catalytic hydrogenolysis, simultaneously of the benzyl and benzylidene groups, gave the desired products that were characterized by 1H and 13C NMR spectroscopy

  synthesis, oligosaccharide, serotype, O-antigen, O antigen, fragment, Vibrio, Vibrio cholerae, Vibrio cholerae O1, methyl, synthetic oligosaccharides, N-iodosuccinimide silver triflate-, promoted glycosylation, tetronic acid

  NCBI PubMed ID: 9210300
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: NIDDK, National Institutes of Health, Bethesda, MD, USA
  
   
  
  Vibrio cholerae O1
  CSDB ID 6166 (all data & tools)
• Article ID: 1396
  Bystricky S, Szu SC, Zhang J, Kovác P "Conformational differences among mono- and oligosaccharide fragments of the O-specific polysaccharides of Vibrio cholerae O1 revealed by circular dichroism" - Carbohydrate Research 314(1-2) (1998) 135-139
  

  The circular dichroism (CD) of synthetic mono- and oligosaccharides that represent the terminal, non-reducing group of O-antigens of Vibrio cholerae O1 from the subtypes Ogawa and Inaba was measured in various solvents. We found differences in the CD of the monosaccharides of these subtypes that decrease with increasing chain lengths of the oligosaccharides. The differences can be explained by different orientations of the N-acyl side chain of the terminal monosaccharides. The linear relationship of ellipticity versus the number of residues in an oligosaccharide chain follows the principle of optical superposition. This, together with a similar contribution by internal units to the overall ellipticity, suggests an identical, regular conformation of oligosaccharide fragments of both Ogawa and Inaba series.

  oligosaccharide, polysaccharide, polysaccharides, conformational, O-antigens, O-specific, O-specific polysaccharide, difference, fragment, Vibrio, Vibrio cholerae, Vibrio cholerae O1, O-specific polysaccharides, circular dichroism

  NCBI PubMed ID: 10230041
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovak Republic
  Methods: CD
  
   
  
  Vibrio cholerae O1
  CSDB ID 6623 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 412
  Wang J, Villeneuve S, Zhang J, Lei PS, Miller CE, Lafaye P, Nato F, Szu SSC, Karpas A, Bystricky S, Robbins JB, Kovác P, Fournier JM, Glaudemans CPJ "On the antigenic determinants of the lipopolysaccharides of Vibrio cholerae O:1, serotypes Ogawa and Inaba" - Journal of Biological Chemistry 273(5) (1998) 2777-2783
  

  Monoclonal, murine IgG1s S-20-4, A-20-6, and IgA 2D6, directed against Vibrio cholerae O:1 Ogawa-lipopolysaccharide exhibited the same fine specificities and similar affinities for the synthetic methyl α-glycosides of the (oligo)saccharide fragments mimicking the Ogawa O-polysaccharide (O-PS). They did not react with the corresponding synthetic fragments of Inaba O-PS. IgG1s S-20-4 and A-20-6 have absolute affinity constants for synthetic Ogawa mono- to hexasaccharides of from approximately 10(5) to approximately 10(6) M-1. For IgG1s S-20-4, A-20-6, and IgA 2D6, the nonreducing terminal residue of Ogawa O-PS is the dominant determinant, accounting for approximately 90% of the maximal binding energy shown by these antibodies. Binding studies of derivatives of the Ogawa monosaccharide and IgGs S-20-4 and A-20-6 revealed that the C-2 O-methyl group fits into a somewhat flexible antibody cavity and that hydrogen bonds involving the oxygen and, respectively, the OH at the 2- and 3-position of the sugar moiety as well as the 2'-position in the amide side chain are required. Monoclonal IgA ZAC-3 and IgG3 I-24-2 are specific for V. cholerae O:1 serotypes Ogawa/Inaba-LPS.1 The former did not show binding with members of either series of the synthetic ligands related to the O-antigens of the Ogawa or Inaba serotypes, in agreement with its reported specificity for the lipid/core region (1). Inhibition studies revealed that the binding of purified IgG3 I-24-2 to Ogawa-LPS might be mediated by a region in the junction of the OPS to the lipid-core region of the LPS. cDNA cloning and analysis of the anti-Ogawa antibodies S-20-4, A-20-6, and 2D6 revealed a very high degree of homology among the heavy chains. Among the light chains, no such homology between S-20-4 and A-20-6 on the one hand, and 2D6 on the other hand, exists. For the anti-Inaba/Ogawa antibodies I-24-2 and ZAC-3, their heavy chains are completely different, with some homology among the light chains

  Lipopolysaccharide, lipopolysaccharides, LPS, serotype, antigenic, antigenic determinant, determinant, Serotypes, Vibrio, Vibrio cholerae

  NCBI PubMed ID: 9446585
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: glau@helix.nih.gov
  Institutions: Laboratory of Medicinal Chemistry, NIDDK and the Laboratory of Developmental and Molecular Immunity, NICHD, National Institutes of Health, Bethesda, MD, USA, Unite du Cholera et des Vibrions, Centre National de Reference des Vibrions et du Cholera and Hybridolab, Institut Pasteur, Paris, France
  Methods: 1H NMR, PCR, DNA sequencing, SDS-PAGE, ELISA, genetic methods
  
   
  
  Vibrio cholerae O1 Ogawa
  CSDB ID 8784 (all data & tools)
• Article ID: 1323
  Zhang J, Kovác P "Synthesis of methyl a-glycosides of some higher oligosaccharide fragments of the O-antigen of Vibrio cholerae O1, serotype Inaba and Ogawa" - Carbohydrate Research 300(4) (1997) 329-339
  

  The title oligosaccharides, the tri- through the hexasaccharide in the Inaba series and the penta- and the hexasaccharide in the Ogawa series, have been synthesized using 1-thioglycosides of precursors to 3-O-benzyl-perosamine (4-amino-4,6-dideoxy-D-mannose) as building blocks and N-iodosuccinimide/silver triflate as a promoter. The azido groups in the assembled oligosaccharides were reduced to amino groups, which were then acylated using 2,4-O-benzylidene-3-deoxy-L-glycero-tetronic acid as the derivatizing reagent. Catalytic hydrogenolysis, simultaneously of the benzyl and benzylidene groups, gave the desired products that were characterized by 1H and 13C NMR spectroscopy

  synthesis, oligosaccharide, serotype, O-antigen, O antigen, fragment, Vibrio, Vibrio cholerae, Vibrio cholerae O1, methyl, synthetic oligosaccharides, N-iodosuccinimide silver triflate-, promoted glycosylation, tetronic acid

  NCBI PubMed ID: 9210300
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: NIDDK, National Institutes of Health, Bethesda, MD, USA
  
   
  
  Vibrio cholerae O1
  CSDB ID 6167 (all data & tools)
• Article ID: 1396
  Bystricky S, Szu SC, Zhang J, Kovác P "Conformational differences among mono- and oligosaccharide fragments of the O-specific polysaccharides of Vibrio cholerae O1 revealed by circular dichroism" - Carbohydrate Research 314(1-2) (1998) 135-139
  

  The circular dichroism (CD) of synthetic mono- and oligosaccharides that represent the terminal, non-reducing group of O-antigens of Vibrio cholerae O1 from the subtypes Ogawa and Inaba was measured in various solvents. We found differences in the CD of the monosaccharides of these subtypes that decrease with increasing chain lengths of the oligosaccharides. The differences can be explained by different orientations of the N-acyl side chain of the terminal monosaccharides. The linear relationship of ellipticity versus the number of residues in an oligosaccharide chain follows the principle of optical superposition. This, together with a similar contribution by internal units to the overall ellipticity, suggests an identical, regular conformation of oligosaccharide fragments of both Ogawa and Inaba series.

  oligosaccharide, polysaccharide, polysaccharides, conformational, O-antigens, O-specific, O-specific polysaccharide, difference, fragment, Vibrio, Vibrio cholerae, Vibrio cholerae O1, O-specific polysaccharides, circular dichroism

  NCBI PubMed ID: 10230041
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: Institute of Chemistry, Slovak Academy of Sciences, Bratislava, Slovak Republic
  Methods: CD
  
   
  
  Vibrio cholerae O1
  CSDB ID 6624 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: 5-carboxypentyl or 2-[2-(carboxy)ethylthio]ethyl or 5-hydrozinocarbonylpentyl or 2-[2-(hydrozinocarbonyl)ethylthio]ethyl
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 1064
  Ogawa Y, Lei P, Kovác P "Synthesis of eight glycosides of hexasaccharide fragments representing the terminus of the O-polysaccharide of Vibrio cholerae O:1, serotype Inaba and Ogawa, bearing aglycons suitable for linking to proteins" - Carbohydrate Research 293 (1996) 173-194
  

  The title substances were prepared from intermediate, fully acetylated α-trimethylsilylethyl (SE) glycosides. The latter were assembled in a blockwise manner, using as the glycosyl donor the α-glycosyl chloride of a disaccharide bearing two 4-azido-4-deoxy functions. Next, the azido groups in the assembled hexasaccharides were converted to the corresponding amines, and these were acylated with 4-O-benzyl-3-deoxy-L-glycero-tetronic acid in the presence of a water-soluble carbodiimide. The SE glycosides were then transformed to glycosyl imidates, and these were coupled with methyl 6-hydroxyhexanoate or methyl 2-(2-hydroxyethylthio) propionate. The aglycons in the glycosides thus obtained were then converted to the corresponding carboxylic acids or acyl hydrazides. Such compounds are suitable for linking to proteins to obtain neoglycoproteins.

  synthesis, hexasaccharide, serotype, protein, O-polysaccharide, fragment, Vibrio, Vibrio cholerae O1, proteins, glycosides, glycoside, terminus, neoglycoside, 4-O-benzyl-3-deoxy-L-glycero-tetronic acid

  NCBI PubMed ID: 8938375
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: NIDDK, National Institutes of Health, Bethesda, MD, USA
  
   
  
  Vibrio cholerae O1 Ogawa
  CSDB ID 3892 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: linker
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 1328
  Zhang JA, Kovác P "Studies on vaccines against cholera. Synthesis of neoglycoconjugates from the hexasaccharide determinant of Vibrio cholerae O:1, serotype Ogawa, by single-point attachment or by attachment of the hapten in the form of clusters" - Carbohydrate Research 321(3-4) (1999) 157-167
  

  The terminal hexasaccharide of the O-antigen of Vibrio cholerae O:1, serotype Ogawa, has been synthesized in the form of a glycoside whose aglycon (linker) allows conjugation to carrier proteins by reductive amination. The conjugate obtained from direct, single-point attachment of the linker-equipped hapten to chicken serum albumin (CSA) contained seven hapten residues/CSA. A neoglycoconjugate containing the carbohydrate antigen in the form of clusters was obtained using, as a hapten subcarrier, an oligopeptide containing 16 amino groups. It was treated with a limited amount of hapten, to give a hapten-carrying subcarrier (HCS). Subsequent conjugation of HCS to CSA, using squaric acid diethyl ester as a conjugation reagent, gave a cross-linked, glycocluster conjugate containing 51% (w/w) of the carbohydrate

  synthesis, oligosaccharide, hexasaccharide, serotype, determinant, form, cluster, vaccines, Vibrio, hapten, Vibrio cholerae, vaccine, cholera, glycoconjugate, attachment, neoglycoconjugate, glycocluster, subcarrier, synthetic vaccine

  NCBI PubMed ID: 10614066
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Institutions: National Institutes of Health, NIDDK, Laboratory of Medicinal Chemistry, Bethesda, MD 20892-0815, USA
  
   
  
  Vibrio cholerae O1
  CSDB ID 6170 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: different spacer-BSA
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 1399
  Chernyak A, Karavanov A, Ogawa Y, Kovác P "Conjugating oligosaccharides to proteins by squaric acid diester chemistry: rapid monitoring of the progress of conjugation, and recovery of the unused ligand" - Carbohydrate Research 330(4) (2001) 479-486
  

  oligosaccharide, chemistry, acid, Oligosaccharides, protein, ligand, proteins, recovery

  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: aak@ciphergen.com; kpn@helix.nih.gov
  Institutions: NIDDK, National Institutes of Health, Bethesda, MD, USA, Ciphergen Biosystems, Fremont, CA, USA
  
   
  
  Vibrio cholerae O1
  CSDB ID 6525 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: 5-methoxycarbonylpentyl or linker-BSA
Trivial name: O-antigen fragment
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 1644
  Saksena, Ma X, Wade TK, Kovác P, Wade WF "Effect of saccharide length on the immunogenicity of neoglycoconjugates from synthetic fragments of the O-SP of Vibrio cholerae O1, serotype Ogawa" - Carbohydrate Research 340(14) (2005) 2256-2269
  

  A synthetic hexasaccharide, identical to the terminal hexasaccharide of Ogawa LPS, coupled to bovine serum albumin induced protective antibodies in mice. To determine if there was a minimum saccharide length required for immunogenicity and efficacy, shorter (mono- to pentasaccharide) neoglycoconjugates (CHO-BSA) were tested in mice. The Ogawa CHO-BSA was inoculated at either a constant mass but differing moles, or equal moles but differing masses. Humoral responses were essentially the same when mice received 9 microg of the carbohydrate (0.007 mM with the pentasaccharide) in each of the neoglycoconjugates prepared from mono- through the pentasaccharide, or the same molar amount (0.007 mM), proportionally less by weight when going from the penta- to the monosaccharide. These data show that, within this dose range, the responses occurred virtually independently of the amount of immunogen. Humoral antibodies induced by these immunogens were generally not vibriocidal. Selected antisera induced by CHO-BSA immunogens were protective, but the ELISA titers of the sera were not predictive of the protective capacity. Purified, Ogawa LPS induced anti-Ogawa LPS IgM antibody titers similar to those induced by the Ogawa CHO-BSA conjugates. The anti-whole LPS sera were strongly vibriocidal, as were the previously reported sera induced by hexasaccharide conjugates. This suggests either that the shorter oligosaccharides lack a conformational epitope provided by the hexasaccharide or that the LPS has additional B cell epitopes or selects different B cells in the primary response.

  LPS, Vibrio cholerae O1, conjugate, Ogawa, neoglycoconjugate, Cholera vaccine

  NCBI PubMed ID: 16098493
  Journal NLM ID: 0043535
  Publisher: Elsevier
  Correspondence: william.wade@dartmouth.edu
  Institutions: National Institutes of Health, NIDDK, Laboratory of Medicinal Chemistry, Bethesda, MD, USA, Department of Microbiology and Immunology, Dartmouth Medical School, 630W. Borwell Bldg., Lebanon, NH 03756, USA
  Methods: chemical synthesis
  
   
  
  Vibrio cholerae O1 Ogawa
  CSDB ID 10767 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: MeOOC(CH2)5 or linker-BSA
Trivial name: synthetic hexasaccharide fragment of Ogawa O-antigen
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 3213
  Saksena R, Ma X, Wade TK, Kovác P, Wade WF "Length of the linker and the interval between immunizations influences the efficacy of Vibrio cholerae O1, Ogawa hexasaccharide neoglycoconjugates" - FEMS Immunology and Medical Microbiology 47(1) (2006) 116-128
  

  Ogawa hexasaccharide neoglycoconjugates induce protective antibodies in mice. Similar Ogawa conjugates but with a longer linker that connects the carrier to shorter saccharides are immunogenic, but generally ineffective at inducing vibriocidal or protective antibodies. The efficacy of Ogawa hexasaccharide neoglycoconjugates of different linker lengths were tested. The majority of mice given immunizations separated by a 14-day gap did not produce vibriocidal or protective antibodies. Mice immunized 28 days apart with immunogens containing the shortest or medium length linker, but not the longest, produced vibriocidal and protective antibodies. A nonprotective, priming dose of purified Ogawa LPS followed 5 days later with a booster of the Ogawa neoglycoconjugates (di-, tetra-, or hexasaccharide) resulted in vibriocidal antibodies at day 10.

  Vibrio cholerae, Cholera vaccine, Ogawa lipopolysaccharide

  NCBI PubMed ID: 16706794
  Publication DOI: 10.1111/j.1574-695X.2006.00071.x
  Journal NLM ID: 9315554
  Publisher: Elsevier
  Correspondence: William F. Wade
  Institutions: National Institutes of Health, NIDDK, Laboratory of Medicinal Chemistry, Bethesda, MD, USA
  Methods: serological methods
  
   
  
  Vibrio cholerae O1 Ogawa
  CSDB ID 21208 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: spacer-BSA
Trivial name: Ogawa neoglycoconjugate
Compound class: neoglycoconjugate
Contained glycoepitopes: IEDB_161054,IEDB_161056,IEDB_161058

• Article ID: 3770
  Rollenhagen JE, Kalsy A, Saksena R, Sheikh A, Alam MM, Qadri F, Calderwood SB, Kovác P, Ryan ET "Transcutaneous immunization with a synthetic hexasaccharide-protein conjugate induces anti-Vibrio cholerae lipopolysaccharide responses in mice" - Vaccine 27(36) (2009) 4917-4922
  

  Antibodies specific for Vibrio cholerae lipopolysaccaride (LPS) are common in humans recovering from cholera, and constitute a primary component of the vibriocidal response, a serum complement-mediated bacteriocidal response correlated with protection against cholera. In order to determine whether transcutaneous immunization (TCI) with a V. cholerae neoglycoconjugate (CHO-BSA) comprised of a synthetic terminal hexasaccharide of the O-specific polysaccharide of V. cholerae O1 (Ogawa) conjugated with bovine serum albumin (BSA) could induce anti-V. cholerae LPS and vibriocidal responses, we applied CHO-BSA transcutaneously in the presence or absence of the immune adjuvant cholera toxin (CT) to mice. Transcutaneously applied neoglycoconjugate elicited prominent V. cholerae specific LPS IgG responses in the presence of CT, but not IgM or IgA responses. CT applied on the skin induced strong IgG and IgA serum responses. TCI with neoglycoconjugate did not elicit detectable vibriocidal responses, protection in a mouse challenge assay, or stool anti-V. cholerae IgA responses, irrespective of the presence or absence of CT. Our results suggest that transcutaneously applied synthetic V. cholerae neoglycoconjugate is safe and immunogenic, but predominantly induces systemic LPS responses of the IgG isotype.

  conjugate, cholera, transcutaneous immunization

  NCBI PubMed ID: 19563890
  Journal NLM ID: 8406899
  Publisher: Elsevier
  Correspondence: E.T. Ryan ; julianne.rollenhagen@med.navy.mil
  Institutions: Division of Infectious Diseases, Massachusetts General Hospital, Boston, MA 02114, USA
  Methods: serological methods, statistical analysis, immunization
  
   
  
  Vibrio cholerae O1
  CSDB ID 23827 (all data & tools)

Show legend Show as text

Structure type: oligomer
Trivial name: OSP-core-spacer-BSA
Compound class: glycoconjugate
Contained glycoepitopes: IEDB_137779,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_161054,IEDB_161056,IEDB_161058,IEDB_2189047,IEDB_983931,SB_192

• Article ID: 4136
  Xu P, Alam MM, Kalsy A, Charles RC, Calderwood SB, Qadri F, Ryan ET, Kovác P "Simple, direct conjugation of bacterial O-SP-core antigens to proteins: development of cholera conjugate vaccines" - Bioconjugate Chemistry 22(10) (2011) 2179-2185
  

  Bacterial O-SP-core antigens can be conjugated to proteins in the same, simple way as synthetic, linker-equipped carbohydrates by applying squaric acid chemistry. Introduction of spacers (linkers) to either O-SP-core antigens or protein carriers, which is involved in commonly applied protocols, is not required. The newly developed method described here consists of preparation of a squaric acid monoester derivative of O-SP-core antigen, utilizing the amino group inherent in the core, and reaction of the monoester with the carrier protein. The intermediate monoester can be easily purified; its conjugation can be monitored by SELDI-TOF mass spectrometry and, thus, readily controlled, since the conjugation can be terminated when the desired carbohydrate-protein ratio is reached. Here, we describe production of conjugates containing the O-SP-core antigen of Vibrio cholerae O1, the major cause of cholera, a severe dehydrating diarrheal disease of humans. The resultant products are recognized by convalescent phase sera from patients recovering from cholera in Bangladesh, and anti-O-SP-core-protein responses correlate with plasma antilipopolysaccharide and vibriocidal responses, which are the primary markers of protection from cholera. The results suggest that such conjugates have potential as vaccines for cholera and other bacterial diseases.

  Vibrio cholerae O1, conjugate vaccine

  NCBI PubMed ID: 21899371
  Publication DOI: 10.1021/bc2001984
  Journal NLM ID: 9010319
  Publisher: Washington, DC: American Chemical Society
  Correspondence: P.K. ; E.T.R.
  Institutions: NIDDK, LBC, National Institutes of Health, Bethesda, MD, USA-0815, United States
  Methods: 13C NMR, mild acid hydrolysis, serological methods, conjugation, SELDI-TOF MS
  
   
  
  Vibrio cholerae O1 Inaba (19479), Vibrio cholerae O1 Ogawa (X-25049)
  CSDB ID 27014 (all data & tools)