Show legend Show as text

Structure type: structural motif or average structure
Compound class: LOS
Contained glycoepitopes: IEDB_130646,IEDB_130651,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_1391964,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144991,IEDB_144998,IEDB_146104,IEDB_146664,IEDB_151528,IEDB_151531,IEDB_152217,IEDB_190606,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_177,SB_178,SB_187,SB_192,SB_195,SB_30,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 2513
  Mandrell RE, Apicella MA "Lipo-oligosaccharides (LOS) of mucosal pathogens: molecular mimicry and host-modification of LOS" - Immunobiology 187 (1993) 382-402
  

  Immunochemical studies of the lipo-oligosaccharides (LOS) of the Gram-negative bacteria Neisseria gonorrhoeae and Neisseria meningitidis have revealed some interesting structural characteristics of these LOS that might relate to their roles during pathogenesis. The carbohydrate moieties of the LOS of pathogenic Neisseria mimic carbohydrates present in glycosphingolipids of human cells. Firstly, an LOS component present among a number of Neisseria species is antigenically and/or chemically identical to lactoneoseries glycosphingolipids present in human cells. The lactoneoseries LOS becomes sialylated on Neisseria gonorrhoeae when they are grown in the presence of cytidine 5'-monophospho-N-acetyl-neuraminic acid (CMP-NANA), the nucleotide sugar for sialic acid. Examination of gonococci present in exudates from males with natural infection indicates that sialylation also occurs in vivo. The mechanism for this process apparently involves a bacterial sialyltransferase scavenging available host CMP-NANA ("host-modification" of LOS) and transferring the sialic acid to the lactoneoserieslike LOS. Strains of N. meningitidis and Haemophilus influenzae also express similarly sialylated LOS suggesting that this is a common mechanism of pathogenesis among these bacteria. Additional examples of LOS that mimic other glycosphingolipid series have been identified also and the fact that multiple series can be expressed in a single population of gonococci suggests that a diverse set of LOS can be presented to the host during infection. It is possible that this diverse set of LOS serve different functions for the bacteria in various hosts and/or environments during infection.

  NCBI PubMed ID: 8330904
  Publication DOI: 10.1016/S0171-2985(11)80352-9
  Journal NLM ID: 8002742
  Publisher: Amsterdam: Elsevier
  Institutions: Division of Infectious Diseases, San Francisco General Hospital, University of California
  
   
  
  Neisseria gonorrhoeae
  CSDB ID 129900 (all data & tools)

Show legend Show as text

Structure type: oligomer
Compound class: core oligosaccharide
Contained glycoepitopes: IEDB_130646,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_137776,IEDB_1391966,IEDB_140108,IEDB_140110,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142351,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144991,IEDB_146104,IEDB_146664,IEDB_149144,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_423101,IEDB_742247,IEDB_983931,SB_145,SB_165,SB_166,SB_173,SB_177,SB_187,SB_192,SB_195,SB_21,SB_30,SB_31,SB_6,SB_62,SB_7,SB_88

• Article ID: 4038
  Houliston RS, Vinogradov E, Dzieciatkowska M, Li J, St Michael F, Karwaski MF, Brochu D, Jarrell HC, Parker CT, Yuki N, Mandrell RE, Gilbert M "Lipooligosaccharide of Campylobacter jejuni: Similarity with multiple types of mammalian glycans beyond gangliosides" - Journal of Biological Chemistry 286(14) (2011) 12361-12370
  

  Campylobacter jejuni is well known for synthesizing ganglioside mimics within the glycan component of its lipooligosaccharide (LOS), which have been implicated in triggering Guillain-Barre syndrome. We now confirm that this pathogen is capable of synthesizing a much broader spectrum of host glycolipid/glycoprotein mimics within its LOS. P blood group and paragloboside (lacto-N-neotetraose) antigen mimicry is exhibited by RM1221, a strain isolated from a poultry source. RM1503, a gastroenteritis-associated strain, expresses lacto-N-biose and sialyl-Lewis c units, the latter known as the pancreatic tumor-associated antigen, DU-PAN-2 (or LSTa). C. jejuni GC149, a Guillain-Barre syndrome-associated strain, expresses an unusual sialic acid-containing hybrid oligosaccharide with similarity to both ganglio and P(k) antigens and can, through phase variation of its LOS biosynthesis genes, display GT1a or GD3 ganglioside mimics. We show that the sialyltransferase CstII and the galactosyltransferase CgtD are involved in the synthesis of multiple mimic types, with LOS structural diversity achieved through evolving allelic substrate specificity.

  Lipooligosaccharide, Campylobacter jejuni, gangliosides, mimicry

  NCBI PubMed ID: 21257763
  Publication DOI: 10.1074/jbc.M110.181750
  Journal NLM ID: 2985121R
  Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
  Correspondence: michel.gilbert@nrc-cnrc.gc.ca
  Institutions: From the Institute for Biological Sciences, National Research Council, Ottawa, Ontario K1A 0R6, Canada
  Methods: 13C NMR, 1H NMR, NMR-2D, methylation, GC-MS, sugar analysis, 31P NMR, NMR-1D, genetic methods, de-N-O-acylation, CE, LC-MS
  
   
  
  Campylobacter jejuni RM1221
  CSDB ID 26226 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: Asn
Compound class: N-glycan
Contained glycoepitopes: IEDB_115013,IEDB_123886,IEDB_130645,IEDB_130646,IEDB_130649,IEDB_130651,IEDB_130701,IEDB_131186,IEDB_134624,IEDB_135813,IEDB_135815,IEDB_135818,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140122,IEDB_141496,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_144983,IEDB_144987,IEDB_144991,IEDB_146104,IEDB_146694,IEDB_149558,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_153201,IEDB_153212,IEDB_156493,IEDB_167072,IEDB_190606,IEDB_221845,IEDB_241097,IEDB_418918,IEDB_548907,IEDB_689191,IEDB_742245,IEDB_742247,IEDB_742248,IEDB_918314,IEDB_983930,SB_163,SB_165,SB_166,SB_177,SB_187,SB_195,SB_197,SB_198,SB_30,SB_31,SB_33,SB_40,SB_44,SB_62,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_87,SB_88

• Article ID: 6019
  Veríssimo CD, Graeff-Teixeira C, Jones MK, Morassutti AL "Glycans in the roles of parasitological diagnosis and host-parasite interplay" - Parasitology 146(10) (2019) 1217-1232
  

  The investigation of the glycan repertoire of several organisms has revealed a wide variation in terms of structures and abundance of glycan moieties. Among the parasites, it is possible to observe different sets of glycoconjugates across taxa and developmental stages within a species. The presence of distinct glycoconjugates throughout the life cycle of a parasite could relate to the ability of that organism to adapt and survive in different hosts and environments. Carbohydrates on the surface, and in excretory-secretory products of parasites, play essential roles in host-parasite interactions. Carbohydrate portions of complex molecules of parasites stimulate and modulate host immune responses, mainly through interactions with specific receptors on the surface of dendritic cells, leading to the generation of a pattern of response that may benefit parasite survival. Available data reviewed here also show the frequent aspect of parasite immunomodulation of mammalian responses through specific glycan interactions, which ultimately makes these molecules promising in the fields of diagnostics and vaccinology.

  immune response, glycoconjugate, glycans, Parasite, protozoa, helminth

  NCBI PubMed ID: 31057132
  Publication DOI: 10.1017/S0031182019000465
  Journal NLM ID: 0401121
  Publisher: London, New York, Cambridge University Press
  Correspondence: Alessandra Loureiro Morassutti
  Institutions: Escola de Ciências, Pontifícia Universidade Católica do Rio Grande do Sul, Av. Ipiranga 6681, Porto Alegre RS 90619-900 Rio Grande do Sul, Brazil, School of Biological Sciences, Queen's University Belfast, 2017, University Road, Belfast, BT7 1NN, Northern Ireland, UK, School of Veterinary Science, University of Queensland, St Lucia, Qld, 4072 Brisbane, Australia
  
   
  
  Trypanosoma brucei
  CSDB ID 29169 (all data & tools)

Show legend Show as text

Structure type: oligomer
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130646,IEDB_130651,IEDB_130654,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136104,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_141829,IEDB_142489,IEDB_143632,IEDB_144562,IEDB_144983,IEDB_144987,IEDB_144991,IEDB_145003,IEDB_145668,IEDB_145669,IEDB_146104,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149557,IEDB_150092,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_167070,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_221845,IEDB_423128,IEDB_461720,IEDB_540672,IEDB_548907,IEDB_742247,IEDB_983930,SB_136,SB_157,SB_165,SB_166,SB_177,SB_187,SB_195,SB_196,SB_197,SB_198,SB_30,SB_31,SB_33,SB_44,SB_62,SB_67,SB_7,SB_72,SB_73,SB_74,SB_85,SB_86,SB_88

• Article ID: 10375
  van Huystee RB, Sesto PA, O'Donell JP "Number and size of oligosaccharides linked to peanut peroxidases" - Plant Physiology and Biochemistry 30 (1992) 147-152
  
  Journal NLM ID: 9882449
  Publisher: Elsevier Science for Société Française De Physiologie Végétale
  
   
  
  Arachis hypogaea
  CSDB ID 147119 (all data & tools)

Show legend Show as text

Structure type: oligomer
Aglycon: (->4) Asn-X-Ser/Thr (major cationic peanut peroxidase)
Compound class: N-glycan
Contained glycoepitopes: IEDB_114701,IEDB_115005,IEDB_115015,IEDB_116644,IEDB_122244,IEDB_123886,IEDB_123887,IEDB_123888,IEDB_130646,IEDB_130651,IEDB_130654,IEDB_130701,IEDB_135813,IEDB_136044,IEDB_136045,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_137485,IEDB_140108,IEDB_140116,IEDB_140122,IEDB_141793,IEDB_141794,IEDB_141807,IEDB_142489,IEDB_144562,IEDB_144983,IEDB_144987,IEDB_144991,IEDB_145003,IEDB_145668,IEDB_145669,IEDB_146104,IEDB_148491,IEDB_148492,IEDB_148493,IEDB_149135,IEDB_149557,IEDB_150092,IEDB_151528,IEDB_151531,IEDB_152206,IEDB_152214,IEDB_153212,IEDB_164174,IEDB_167070,IEDB_167188,IEDB_174332,IEDB_174333,IEDB_190606,IEDB_221845,IEDB_461720,IEDB_548907,IEDB_742247,IEDB_983930,SB_157,SB_165,SB_166,SB_177,SB_187,SB_195,SB_197,SB_198,SB_30,SB_31,SB_33,SB_44,SB_62,SB_67,SB_7,SB_72,SB_73,SB_74,SB_77,SB_85,SB_86,SB_88

• Article ID: 11040
  van Huystee RB, McManus MT "Glycans of higher plant peroxidases: recent observations and future speculations" - Glycoconjugate Journal 15(2) (1998) 101-106
  

  Plant peroxidases are composed of a peptide and associated heme, calcium and glycans. The 3D structure of the major cationic peanut peroxidase has revealed the sites of the heme and calcium. But the diffraction of the glycans was not sufficient to show their structure. This review presents research that has been executed to obtain putative glycans and their binding sites, and to gain an indirect insight into these glycans. It also offers approaches that will be used to determine the function of the glycans on the peanut peroxidase. Some comparisons are made with other plant glycoproteins including peroxidases from plants other than peanut.

  glycans, plant peroxidases

  NCBI PubMed ID: 9557869
  Publication DOI: 10.1023/a:1006955903531
  Journal NLM ID: 8603310
  Publisher: Kluwer Academic Publishers
  Institutions: Department of Plant Sciences, The University of Western Ontario London, Ontario, Canada, Department of Plant Biology and Biotechnology, Massey University, Palmerston North, New Zealand
  
   
  
  Arachis hypogaea
  CSDB ID 61357 (all data & tools)