Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Salmonella choleraesuis SN57, Salmonella typhimurium TV119
  CSDB ID 7761 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130693,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli EH100
  CSDB ID 31501 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli F653
  CSDB ID 31502 (all data & tools)

Show legend Show as text

Structure type: fragment of a bigger structure
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_135813,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140529,IEDB_141794,IEDB_141807,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_232584,IEDB_983931,SB_192,SB_7

• Article ID: 339
  Nnalue NA, Khan GN, Mustafa N "Cross-reactivity between six Enterobacteriaceae complete lipopolysaccharide core chemotypes" - Journal of Medical Microbiology 48(5) (1999) 433-441
  

  To gain insight into the value of lipopolysaccharide (LPS) core determinants for cross-protective immunisation the serological relationships between six complete (LPS) core types from Enterobacteriaceae were investigated. Hyperimmune sera were raised in mice by repeated immunisation with heat-killed strains of Salmonella choleraesuis (Ra core type) or Escherichia coli (core types R1, R2, R3, R4 and K12) and characterised for reactivity with complete and incomplete core chemotypes by ELISA and immunoblotting. Three sera (anti-Ra, anti-R2 and anti-R3) reacted strongly with 3-5 different complete core types whereas the other three (anti-R1, anti-R4 and anti-K12) reacted strongly only with their homologous core types in these assays. Two approaches were used to examine further the structural bases for cross-reactivity between these cores. By the first approach the anti-complete-core sera were tested for cross-reactivity with truncated forms of the Salmonella species core (incomplete cores) derived from core-defective mutants. By the second approach, antisera raised against some core-defective mutants were tested for cross-reactivity with complete cores. The results of these investigations revealed that several pair-wise combinations of core types can be used as immunogens to elicit immune responses that recognise all six core types and that the major determinants which mediate cross-reactivity between complete cores are localised in the outer core region.

  Lipopolysaccharide, core, lipopolysaccharide core, chemotype, Chemotypes, cross-reactivity, crossreactivity, Enterobacteriaceae

  NCBI PubMed ID: 10229540
  Journal NLM ID: 0224131
  Publisher: Reading, England: Society for General Microbiology
  Institutions: Department of Medical Microbiology, Faculty of Medicine and Health Sciences, United Arab Emirates University, Al Ain, United Arab Emirates
  Methods: SDS-PAGE, ELISA, biological assays, serological methods, immunoblotting
  
   
  
  Escherichia coli W3110
  CSDB ID 31504 (all data & tools)

Show legend Show as text

Structure type: polymer chemical repeating unit ; n=10-15
Aglycon: Asn of a protein end: AlaNH2-Asn-Ala-Ser-...
Compound class: N-glycan
Contained glycoepitopes: IEDB_130648,IEDB_135813,IEDB_136095,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_141501,IEDB_141584,IEDB_141807,IEDB_149155,IEDB_151531,IEDB_152216,IEDB_190606,IEDB_885822

• Article ID: 468
  Schäffer C, Messner P "Surface-layer glycoproteins: an example for the diversity of bacterial glycosylation with promising impacts on nanobiotechnology" - Glycobiology 14(8) (2004) 31R-42R
  

  Bacterial cell surface layers, referred to simply as S-layers, have been described for all major phylogenetic groups of bacteria, which may indicate their pivotal role for a bacterium in its natural habitat. They have the unique ability to assemble into two-dimensional crystalline arrays that completely cover the bacterial cells. Glycosylation represents the most frequent modification of S-layer proteins. S-layer glycoproteins constitute a class of glycoconjugates first isolated in the mid-1970s, but S-layer glycoprotein research is still being regarded as an 'exotic field of glycobiology,' possibly because of its 'noneukaryotic' character. Extensive work over the past 30 years provided evidence of an enormous diversity of S-layer glycoproteins that have been created in nature over 3 billion years of prokaryotic evolution. These glycoconjugates are substantially different from eukaryotic glycoproteins, with regard to both composition and structure; nevertheless, some general structural concepts may be deduced. The awareness of the high application potential of S-layer glycoproteins, especially in combination with their intrinsic cell surface display feature, in the field of modern nanobiotechnology as a base for glycoengineering has recently led to the investigation of the S-layer protein glycosylation process at the molecular level, which has lagged behind the structural studies due to the lack of suitable molecular tools. From that work an even more interesting picture of this class of glycoconjugates is emerging. The availability of purified enzymes from S-layer glycan biosynthesis pathways exhibiting increased stabilities and/or rare sugar specificities in conjunction with preliminary genomic data on S-layer glycan biosynthesis clusters will pave the way for the rational design of S-layer neoglycoproteins.

  LPS, bacterial glycosylation, genomic glycosylation loci, glycan diversity, glycoengineering, S-layer nanoglycobiology

  NCBI PubMed ID: 15044388
  Publication DOI: 10.1093/glycob/cwh064
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Correspondence: paul.messner@boka.ac.at
  Institutions: Center for NanoBiotechnology, University of Applied Life Sciences and Natural Resources, Gregor-Mendel-Strasse 33, A-1180 Wien, Austria
  
   
  
  Halobacterium halobium R1M1
  CSDB ID 31629 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_419428,IEDB_419429,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 1133
  Ram S, Cox AD, Wright JC, Vogel U, Getzlaff S, Boden R, Li J, Plested JS, Meri S, Gulati S, Stein DC, Richards JC, Moxon ER, Rice PA "Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity" - Journal of Biological Chemistry 278(51) (2003) 50853-50862
  

  We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA on the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that expressed both 3- and 6-PEA simultaneously on HepII did not decrease C4b binding. Glycose chain extension of the first heptose residue (HepI) influenced the nature of the C4b-LOS linkage. Predominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose chain extension of HepI with 3-PEA on HepII in the LOS core. Related LOS species with more truncated chain extensions from HepI bound C4b via amide linkages to 3-PEA on HepII. However, 6-PEA in the LOS core bound C4b even when the glycose chain from HepI bore lacto-N-neotetraose at the terminus. The C4A isoform exclusively formed amide linkages, while C4B bound meningococci preferentially via ester linkages. These data may serve to explain the preponderance of 3-PEA bearing meningococci among clinical isolates because 6-PEA enhances C4b binding that may facilitate clearance of 6-PEA-bearing strains resulting from enhanced serum killing by the classical pathway of complement

  structure, core, heptose, Lipooligosaccharide, Neisseria meningitidis, clinical, disease, isolate, LOS, meningococci, Neisseria, strain, chain, enhanced, infectious disease, specificity, linkage, inner core, medicine, phosphoethanolamine, Infectious, component, binding, lacto-N-neotetraose, acceptor, pathway, serum, bound, bactericidal, serum killing, species, killing, assay, decrease, terminus, amide, target, classical, clearance, complement, ester, pea

  NCBI PubMed ID: 14525973
  Publication DOI: 10.1074/jbc.M308364200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sram@bu.edu
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 02118, Molecular Infectious Diseases Group, Oxford University Department of Pediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom, nstitute for Hygiene and Microbiology, University of Wuerzburg, 97080 Wuerzburg, Germany, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland-00014
  Methods: 1H NMR, ESI-MS, Western blotting
  
   
  
  Neisseria meningitidis MC51, Neisseria meningitidis 2120
  CSDB ID 4313 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_145003,IEDB_146664,IEDB_149144,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_419428,IEDB_419429,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 1133
  Ram S, Cox AD, Wright JC, Vogel U, Getzlaff S, Boden R, Li J, Plested JS, Meri S, Gulati S, Stein DC, Richards JC, Moxon ER, Rice PA "Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity" - Journal of Biological Chemistry 278(51) (2003) 50853-50862
  

  We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA on the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that expressed both 3- and 6-PEA simultaneously on HepII did not decrease C4b binding. Glycose chain extension of the first heptose residue (HepI) influenced the nature of the C4b-LOS linkage. Predominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose chain extension of HepI with 3-PEA on HepII in the LOS core. Related LOS species with more truncated chain extensions from HepI bound C4b via amide linkages to 3-PEA on HepII. However, 6-PEA in the LOS core bound C4b even when the glycose chain from HepI bore lacto-N-neotetraose at the terminus. The C4A isoform exclusively formed amide linkages, while C4B bound meningococci preferentially via ester linkages. These data may serve to explain the preponderance of 3-PEA bearing meningococci among clinical isolates because 6-PEA enhances C4b binding that may facilitate clearance of 6-PEA-bearing strains resulting from enhanced serum killing by the classical pathway of complement

  structure, core, heptose, Lipooligosaccharide, Neisseria meningitidis, clinical, disease, isolate, LOS, meningococci, Neisseria, strain, chain, enhanced, infectious disease, specificity, linkage, inner core, medicine, phosphoethanolamine, Infectious, component, binding, lacto-N-neotetraose, acceptor, pathway, serum, bound, bactericidal, serum killing, species, killing, assay, decrease, terminus, amide, target, classical, clearance, complement, ester, pea

  NCBI PubMed ID: 14525973
  Publication DOI: 10.1074/jbc.M308364200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sram@bu.edu
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 02118, Molecular Infectious Diseases Group, Oxford University Department of Pediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom, nstitute for Hygiene and Microbiology, University of Wuerzburg, 97080 Wuerzburg, Germany, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland-00014
  Methods: 1H NMR, ESI-MS, Western blotting
  
   
  
  Neisseria meningitidis MC51, Neisseria meningitidis 2120
  CSDB ID 4422 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_2189047,IEDB_419429,IEDB_419431,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_6,SB_7,SB_88

• Article ID: 1133
  Ram S, Cox AD, Wright JC, Vogel U, Getzlaff S, Boden R, Li J, Plested JS, Meri S, Gulati S, Stein DC, Richards JC, Moxon ER, Rice PA "Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity" - Journal of Biological Chemistry 278(51) (2003) 50853-50862
  

  We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA on the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that expressed both 3- and 6-PEA simultaneously on HepII did not decrease C4b binding. Glycose chain extension of the first heptose residue (HepI) influenced the nature of the C4b-LOS linkage. Predominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose chain extension of HepI with 3-PEA on HepII in the LOS core. Related LOS species with more truncated chain extensions from HepI bound C4b via amide linkages to 3-PEA on HepII. However, 6-PEA in the LOS core bound C4b even when the glycose chain from HepI bore lacto-N-neotetraose at the terminus. The C4A isoform exclusively formed amide linkages, while C4B bound meningococci preferentially via ester linkages. These data may serve to explain the preponderance of 3-PEA bearing meningococci among clinical isolates because 6-PEA enhances C4b binding that may facilitate clearance of 6-PEA-bearing strains resulting from enhanced serum killing by the classical pathway of complement

  structure, core, heptose, Lipooligosaccharide, Neisseria meningitidis, clinical, disease, isolate, LOS, meningococci, Neisseria, strain, chain, enhanced, infectious disease, specificity, linkage, inner core, medicine, phosphoethanolamine, Infectious, component, binding, lacto-N-neotetraose, acceptor, pathway, serum, bound, bactericidal, serum killing, species, killing, assay, decrease, terminus, amide, target, classical, clearance, complement, ester, pea

  NCBI PubMed ID: 14525973
  Publication DOI: 10.1074/jbc.M308364200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sram@bu.edu
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 02118, Molecular Infectious Diseases Group, Oxford University Department of Pediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom, nstitute for Hygiene and Microbiology, University of Wuerzburg, 97080 Wuerzburg, Germany, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland-00014
  Methods: 1H NMR, ESI-MS, Western blotting
  
   
  
  Neisseria meningitidis 89I
  CSDB ID 4423 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130646,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391966,IEDB_140087,IEDB_140088,IEDB_140089,IEDB_140090,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144998,IEDB_145003,IEDB_146664,IEDB_149144,IEDB_151528,IEDB_151531,IEDB_167070,IEDB_190606,IEDB_2189047,IEDB_419429,IEDB_419431,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_187,SB_192,SB_195,SB_30,SB_6,SB_7,SB_88

• Article ID: 1133
  Ram S, Cox AD, Wright JC, Vogel U, Getzlaff S, Boden R, Li J, Plested JS, Meri S, Gulati S, Stein DC, Richards JC, Moxon ER, Rice PA "Neisserial lipooligosaccharide is a target for complement component C4b: Inner core phosphoethanolamine residues define C4b linkage specificity" - Journal of Biological Chemistry 278(51) (2003) 50853-50862
  

  We identified Neisseria meningitidis lipooligosaccharide (LOS) as an acceptor for complement component C4b (C4b). Phosphoethanolamine (PEA) residues on the second heptose (HepII) residue in the LOS core structure formed amide linkages with C4b. PEA on the 6-position of HepII (6-PEA) was more efficient than 3-PEA in binding C4b. Strains bearing 6-PEA bound more C4b than strains with 3-PEA and were more susceptible to complement-mediated killing in serum bactericidal assays. Deleting 3-PEA from a strain that expressed both 3- and 6-PEA simultaneously on HepII did not decrease C4b binding. Glycose chain extension of the first heptose residue (HepI) influenced the nature of the C4b-LOS linkage. Predominantly ester C4b-LOS bonds were seen when lacto-N-neotetraose formed the terminus of the glycose chain extension of HepI with 3-PEA on HepII in the LOS core. Related LOS species with more truncated chain extensions from HepI bound C4b via amide linkages to 3-PEA on HepII. However, 6-PEA in the LOS core bound C4b even when the glycose chain from HepI bore lacto-N-neotetraose at the terminus. The C4A isoform exclusively formed amide linkages, while C4B bound meningococci preferentially via ester linkages. These data may serve to explain the preponderance of 3-PEA bearing meningococci among clinical isolates because 6-PEA enhances C4b binding that may facilitate clearance of 6-PEA-bearing strains resulting from enhanced serum killing by the classical pathway of complement

  structure, core, heptose, Lipooligosaccharide, Neisseria meningitidis, clinical, disease, isolate, LOS, meningococci, Neisseria, strain, chain, enhanced, infectious disease, specificity, linkage, inner core, medicine, phosphoethanolamine, Infectious, component, binding, lacto-N-neotetraose, acceptor, pathway, serum, bound, bactericidal, serum killing, species, killing, assay, decrease, terminus, amide, target, classical, clearance, complement, ester, pea

  NCBI PubMed ID: 14525973
  Publication DOI: 10.1074/jbc.M308364200
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: sram@bu.edu
  Institutions: Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada, Department of Cell Biology and Molecular Genetics, University of Maryland, College Park, Maryland 20742, Section of Infectious Diseases, Evans Biomedical Research Center, Boston University Medical Center, Boston, Massachusetts 02118, Molecular Infectious Diseases Group, Oxford University Department of Pediatrics, John Radcliffe Hospital, Oxford OX3 9DU, United Kingdom, nstitute for Hygiene and Microbiology, University of Wuerzburg, 97080 Wuerzburg, Germany, Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, Helsinki, Finland-00014
  Methods: 1H NMR, ESI-MS, Western blotting
  
   
  
  Neisseria meningitidis 89I
  CSDB ID 4424 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: LOS
Contained glycoepitopes: IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_141794,IEDB_141807,IEDB_144987,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_221845,IEDB_742247,SB_165,SB_166,SB_187,SB_195,SB_31,SB_62,SB_7,SB_88

• Article ID: 1298
  Yang QL, Gotschlich EC "Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases" - Journal of Experimental Medicine 183 (1996) 323-327
  

  The lipooligosaccharide (LOS) expressed by gonococci spontaneously varies its structure at high frequency, but the underlying genetic mechanism has not been described. We have previously reported that the genes encoding the glycosyl transferases responsible for the biosynthesis of the variable alpha chain of the LOS of Neisseria gonorrhoeae are located in a locus containing five genes, lgtA, lgtB, lgtC, lgtD, and lgtE. Sequence analysis showed that lgtA, lgtC, and lgtD contained poly-G tracts within the coding frames, leading to the hypothesis that shifts in the number of guanosine residues in the poly-G tracts might be responsible for the high frequency variation in structure of gonococcal LOS. We now provide experimental evidence confirming this hypothesis

  structure, Lipooligosaccharide, gene, LOS, tract, variation, transferase, lgt, glycosyl, alteration, gonococcal, transferases, glycosyl transferases

  NCBI PubMed ID: 8551240
  Journal NLM ID: 2985109R
  Publisher: Rockefeller University Press
  Institutions: Laboratory of Bacterial Pathogenesis and Immunology, Rockefeller University, New York, NY, USA
  
   
  
  Neisseria gonorrhoeae 1291b
  CSDB ID 6048 (all data & tools)

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Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_131174,IEDB_133754,IEDB_135610,IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_144825,IEDB_151531,IEDB_225177,IEDB_885823

• Article ID: 1317
  Zdorovenko EL, Zatonsky GV, Kocharova NA, Shashkov AS, Knirel YA, Ovod V "Structures of the O-polysaccharides of two strains of Pseudomonas syringae pv. porri from genomospecies 4" - European Journal of Biochemistry 270(1) (2003) 20-27
  

  Strains of Pseudomonas syringae pv. porri are characterized by a number of pathovar-specific phenotypic and genomic characters and constitute a highly homogeneous group. Using monoclonal antibodies, they all were classified in a novel P. syringae serogroup O9. The O polysaccharides (OPS) isolated from the lipopolysaccharides (LPS) of P. syringae pv. porri NCPPB 3365 and NCPPB 3364T possess multiple oligosaccharide O repeats, some of which are linear and composed of l-rhamnose (l-Rha), whereas the major O repeats are branched with l-rhamnose in the main chain and GlcNAc in side chains (structures 1 and 2). Both branched O repeats, which differ in the position of substitution of one of the Rha residues and in the site of attachment of GlcNAc, were found in the two strains studied, O repeat 1 being major in strain NCPPB 3365 and 2 in strain NCPPB 3364T. [formula: see text]. The relationship between OPS chemotype and serotype on one hand and the genomic characters of P. syringae pv. porri and other pathovars delineated in genomospecies 4 on the other hand is discussed

  Lipopolysaccharide, monoclonal antibody, serological classification, Pseudomonas syringae, O polysaccharide structure

  NCBI PubMed ID: 12492471
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: knirel@ioc.ac.ru
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Institute of Medical Technology, University of Tampere, Tampere, Finland
  Methods: methylation, NMR-2D, NMR, Smith degradation
  
   
  
  Pseudomonas syringae pv. ribicola NCPPB1010
  CSDB ID 6123 (all data & tools)

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Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide
Contained glycoepitopes: IEDB_131174,IEDB_133754,IEDB_135610,IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_225177,IEDB_885823

• Article ID: 1317
  Zdorovenko EL, Zatonsky GV, Kocharova NA, Shashkov AS, Knirel YA, Ovod V "Structures of the O-polysaccharides of two strains of Pseudomonas syringae pv. porri from genomospecies 4" - European Journal of Biochemistry 270(1) (2003) 20-27
  

  Strains of Pseudomonas syringae pv. porri are characterized by a number of pathovar-specific phenotypic and genomic characters and constitute a highly homogeneous group. Using monoclonal antibodies, they all were classified in a novel P. syringae serogroup O9. The O polysaccharides (OPS) isolated from the lipopolysaccharides (LPS) of P. syringae pv. porri NCPPB 3365 and NCPPB 3364T possess multiple oligosaccharide O repeats, some of which are linear and composed of l-rhamnose (l-Rha), whereas the major O repeats are branched with l-rhamnose in the main chain and GlcNAc in side chains (structures 1 and 2). Both branched O repeats, which differ in the position of substitution of one of the Rha residues and in the site of attachment of GlcNAc, were found in the two strains studied, O repeat 1 being major in strain NCPPB 3365 and 2 in strain NCPPB 3364T. [formula: see text]. The relationship between OPS chemotype and serotype on one hand and the genomic characters of P. syringae pv. porri and other pathovars delineated in genomospecies 4 on the other hand is discussed

  Lipopolysaccharide, monoclonal antibody, serological classification, Pseudomonas syringae, O polysaccharide structure

  NCBI PubMed ID: 12492471
  Journal NLM ID: 0107600
  Publisher: Oxford, UK: Blackwell Science Ltd. on behalf of the Federation of European Biochemical Societies
  Correspondence: knirel@ioc.ac.ru
  Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Institute of Medical Technology, University of Tampere, Tampere, Finland
  Methods: methylation, NMR-2D, NMR, Smith degradation
  
   
  
  Pseudomonas syringae pv. ribicola NCPPB1010
  CSDB ID 6124 (all data & tools)

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Structure type: oligomer
Aglycon: core-lipid A
Contained glycoepitopes: IEDB_130644,IEDB_130646,IEDB_130654,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_143250,IEDB_144562,IEDB_145669,IEDB_149555,IEDB_149557,IEDB_149561,IEDB_150092,IEDB_150948,IEDB_151531,IEDB_152214,IEDB_153553,IEDB_174333,IEDB_190606,IEDB_461719,IEDB_461720,IEDB_461721,SB_147,SB_154,SB_157,SB_165,SB_166,SB_187,SB_195,SB_30,SB_34,SB_7,SB_86,SB_88

• Article ID: 1357
  Appelmelk BJ, Shiberu B, Trinks C, Tapsi N, Zheng PY, Verboom T, Maaskant J, Hokke CH, Schiphorst WECM, Blanchard D, Simoons-Smit IM, van den Eijnden DH, Vandenbroucke-Grauls CMJE "Phase variation in Helicobacter pylori lipopolysaccharide" - Infection and Immunity 66(1) (1998) 70-76
  

  Lipopolysaccharide, LPS, Phase variation, phase, variation, O-antigen, Helicobacter pylori, Helicobacter, Lewis x, Lewis y

  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, Amterdam, The Netherlands
  
   
  
  Helicobacter pylori var. 1b
  CSDB ID 6388 (all data & tools)

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Structure type: polymer chemical repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_130701,IEDB_135813,IEDB_136035,IEDB_136045,IEDB_137340,IEDB_137485,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_145669,IEDB_150092,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_174333,IEDB_423097,IEDB_983930,SB_44,SB_67,SB_72,SB_86

• Article ID: 1433
  Skurnik M, Peippo A, Ervelä E "Characterization of the O-antigen gene clusters of Yersinia pseudotuberculosis and the cryptic O-antigen gene cluster of Yersinia pestis shows that the plague bacillus is most closely related to and has evolved from Y-pseudotuberculosis serotype O:1b" - Molecular Microbiology 37(2) (2000) 316-330
  

  One of the most virulent and feared bacterial pathogens is Yersinia pestis, the aetiologic agent of bubonic plague. Characterization of the O-antigen gene clusters of 21 serotypes of Yersinia pseudotuberculosis and the cryptic O-antigen gene cluster of Y. pestis showed that the plague bacillus is most closely related to and has evolved from Y. pseudotuberculosis serotype O:1b. The nucleotide sequences of both gene clusters (about 20.5 kb each) were determined and compared to identify the differences that caused the silencing of the Y. pestis gene cluster. At the nucleotide sequence level, the loci were 98.9+ACU- identical and, of the 17 biosynthetic genes identified from the O:1b gene cluster, five were inactivated in the Y. pestis cluster, four by insertions or deletions of one nucleotide and one by a deletion of 62 nucleotides. Apparently, the expression of the O-antigen is not beneficial for the virulence or to the lifestyle of Y. pestis and, therefore, as one step in the evolution of Y. pestis, the O-antigen gene cluster was inactivated.

  gene, characterization, serotype, O-antigen, O antigen, cluster, gene cluster, Yersinia pseudotuberculosis, Bacillus, Yersinia, Yersinia pestis, Plague

  NCBI PubMed ID: 10931327
  Journal NLM ID: 8712028
  Publisher: Blackwell Publishing
  Correspondence: mskurnik@utu.fi
  Institutions: Department of Medical Biochemistry, Institute of Biomedicine, University of Turku, Kiinamyllynkatu 10, 20520 Turku, Finland.
  
   
  
  Yersinia pseudotuberculosis O1b
  CSDB ID 4912 (all data & tools)

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Structure type: oligomer
Trivial name: GIPL, GIPL-1
Compound class: lipophosphoglycan
Contained glycoepitopes: IEDB_130701,IEDB_136095,IEDB_137472,IEDB_141807,IEDB_144983,IEDB_151531,IEDB_152206,IEDB_164174,IEDB_190606,IEDB_983930,SB_197,SB_44,SB_67,SB_72

• Article ID: 1668
  Moody SF "Molecular variation in Leishmania" - Acta Tropica 53 (1993) 185-204
  
  Journal NLM ID: 0370374
  Publisher: Elsevier
  
   
  
  Leishmania major
  CSDB ID 100205 (all data & tools)
• Article ID: 1680
  Avila JL, Rojas M, Rodas A, Convit J "Parasitic oligosaccharide residues recognized by patients with mucocutaneous and localized cutaneous leishmaniasis" - American Journal of Tropical Medicine and Hygiene 47 (1992) 284-290
  

  Humoral immune responses were studied in 118 Venezuelan patients with either active mucocutaneous (MCL) or localized cutaneous leishmaniasis (LCL). Most patients had elevated antibody levels to the six promastigote oligosaccharide residues studied: galactosyl(α 1-2)galactose, galactosyl(α 1-3)galactose, galactosyl(α 1-6)galactose, galactosyl(α 1-3)mannose, galactofuranosyl(β1-3)mannose, and galactocerebroside. Significantly higher antibody levels were found in patients with MCL against galactosyl(α 1-3)galactose and Leishmania tropica glycoinositol phospholipid (GIPL)-1, GIPL-2, and GIPL-3 compared with patients with LCL. For both clinical forms of American cutaneous leishmaniasis (ACL), the most reactive antigen was galactosyl(α 1-3)galactose, with elevated levels found in 63% and 79% of MCL and LCL patients, respectively. In patients with MCL and LCL, no significant relationship was found between antibody levels against a given oligosaccharide residue and clinical parameters such as age, leishmanin diameter, number of skin lesions, or time of evolution. It is noteworthy that 33% and 15% of MCL and LCL patients, respectively, did not have elevated antibody levels against the six different oligosaccharide residues studied. This suggests the presence of a subpopulation of non-humoral immunoreactive ACL patients. The relationship between abnormal levels of oligosaccharide antibodies and the final outcome of the disease remains to be established.

  NCBI PubMed ID: 1524141
  Journal NLM ID: 0370507
  Publisher: Northbrook, IL: American Society of Tropical Medicine and Hygiene
  Institutions: Instituto de Biomedicina, Caracas, Venezuela
  
   
  
  Leishmania major
  CSDB ID 101605 (all data & tools)
• Article ID: 1737
  Schneider P, Rosat JP, Ransijn A, Ferguson MAJ, McConville MJ "Characterization of glycoinositol phospholipids in the amastigote stage of the protozoan parasite Leishmania major" - Biochemical Journal 295 (1993) 555-564
  

  The major macromolecules on the surface of the parasitic protozoan Leishmania major appear to be down-regulated during transformation of the parasite from an insect-dwelling promastigote stage to an intracellular amastigote stage that invades mammalian macrophages. In contrast, the major parasite glycolipids, the glycoinositol phospholipids (GIPLs), are shown here to be expressed at near-constant levels in both developmental stages. The structures of the GIPLs from tissue-derived amastigotes have been determined by h.p.l.c. analysis of the deaminated and reduced glycan head groups, and by chemical and enzymic sequencing. The deduced structures appear to form a complete biosynthetic series, ranging from Man α 1-4GlcN-phosphatidylinositol (PI) to Gal α1-3 Galf β1-3 Man α1-3 Man α1-4 GlcN-PI (GIPL-2). A small proportion of GIPL-2 was further extended by addition of a Gal residue in either α 1-6 or β 1-3 linkage. From g.c.-m.s. analysis and mild base treatment, all the GIPLs were shown to contain either alkylacylglycerol or lyso-alkylglycerol lipid moieties, where the alkyl chains were predominantly C18:0, with lower levels of C20:0, C22:0 and C24:0. L. major amastigotes also contained at least two PI-specific phospholipase C-resistant glycolipids which are absent from promastigotes. These neutral glycolipids were resistant to both mild acid and mild base hydrolysis, contained terminal β-Gal residues and were not lost during extensive purification of amastigotes from host cell membranes. It is likely that these glycolipids are glycosphingolipids acquired from the mammalian host. The GIPL profile of L. major amastigotes is compared with the profiles found in L. major promastigotes and L. donovani amastigotes.

  NCBI PubMed ID: 8240257
  Journal NLM ID: 2984726R
  Publisher: London, UK : Published by Portland Press on behalf of the Biochemical Society
  Institutions: Department of Biochemistry, University of Dundee, UK.
  
   
  
  Leishmania major
  CSDB ID 106334 (all data & tools)
• Article ID: 2503
  de Lederkremer RM, Colli W "Galactofuranose-containing glycoconjugates in trypanosomatids" - Glycobiology 5 (1995) 547-552
  

  Galactofuranose has been characterized in glycoinositolphospholipid (GIPL) anchor-like structures having a glycerolipid or a ceramide, as in lipopeptidophosphoglycan (LPPG) of Trypanosoma cruzi, in the oligosaccharide core of lipopeptidophosphoglycan (LPG) of Leishmania species, and also modifying high-mannose chains of trypanosomatid glycoproteins. Galactofuranose is usually present linked β1→3 to Man, either as a terminal non-reducing unit, like in LPPG, or in the middle of the oligosaccharide core, as in LPG. The presence in protozoan parasites of galactose in the furanose configuration is a feature which deserves further attention since the mammalian hosts do not appear to produce glycoconjugates containing this structural unit. For that reason, hosts produce antibodies against galactofuranose, which may turn out to be important in understanding the pathogenesis and in the development of diagnostic methods. The metabolic pathways involved in the attachment to or removal of galactofuranose from glycoconjugates have not yet been elucidated. This is an area of incipient research, but of growing importance, since it will foster the design of inhibitors which may prove to be useful for the treatment of disease.

  NCBI PubMed ID: 8563141
  Journal NLM ID: 9104124
  Publisher: IRL Press at Oxford University Press
  Institutions: Departamento de Química Orgánica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina
  
   
  
  Leishmania major
  CSDB ID 127658 (all data & tools)