CSDB: Search results

Taxonomic group: protista / Parabasalia (Phylum: Parabasalia)
Host organism: Homo sapiens
Associated disease: infection due to Trichomonas vaginalis [ICD11: XN7YM

]

The structure was elucidated in this paper
NCBI PubMed ID: 21900246
Publication DOI: 10.1074/jbc.M111.280578
Journal NLM ID: 2985121R
Publisher: Baltimore, MD: American Society for Biochemistry and Molecular Biology
Correspondence: m.a.j.ferguson

dundee.ac.uk; johnsonp

ucla.edu
Institutions: Department of Microbiology, Immunology, and Molecular Genetics, UCLA, Los Angeles, California 90095-1489, USA

The extracellular parasite Trichomonas vaginalis contains a surface glycoconjugate that appears to mediate parasite-host cell interaction via binding to human galectin-1. This glycoconjugate also elicits cytokine production from human vaginal epithelial cells, implicating its role in modulation of host immune responses. We have analyzed the structure of this glycoconjugate, previously described to contain the sugars rhamnose (Rha), N-acetylglucosamine (GlcNAc), galactose (Gal), xylose (Xyl), N-acetylgalactosamine (GalNAc), and glucose (Glc), using gas chromatograph mass spectrometry (GC-MS), matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF), electrospray MS/MS, and nuclear magnetic resonance (NMR), combined with chemical and enzymatic digestions. Our data reveal a complex structure, named T. vaginalis lipoglycan (TvLG), that differs markedly from Leishmania lipophosphoglycan and Entamoeba lipopeptidophosphoglycan and is devoid of phosphosaccharide repeats. TvLG is composed of an α1-3 linked polyrhamnose core, where Rha residues are substituted at the 2-position with either β-Xyl or chains of, on average, five N-acetyllactosamine (-3Galβ1-4GlcNAcβ1-) (LacNAc) units and occasionally lacto-N-biose (-3Galβ1-3GlcNAcβ1-) (LNB). These chains are themselves periodically substituted at the Gal residues with Xyl-Rha. These structural analyses led us to test the role of the poly-LacNAc/LNB chains in parasite binding to host cells. We found that reduction of poly-LacNAc/LNB chains decreased the ability of TvLG to compete parasite binding to host cells. In summary, our data provide a new model for the structure of TvLG, composed of a polyrhamnose backbone with branches of Xyl and poly-LacNAc/LNB. Furthermore, the poly-LacNAc side chains are shown to be involved in parasite-host cell interaction.

Pathogenesis, adhesion, glycoconjugate, host-pathogen interactions, glycolipid structure, Trichomonas, TvLG

Structure type: structural motif or average structure
Location inside paper: p. 40506, Fig. 7A
Trivial name: TvLG
Compound class: lipoglycan
Contained glycoepitopes: IEDB_114701,IEDB_130646,IEDB_130655,IEDB_130697,IEDB_135813,IEDB_136044,IEDB_136105,IEDB_137340,IEDB_137472,IEDB_137776,IEDB_1391962,IEDB_140108,IEDB_140122,IEDB_141794,IEDB_141807,IEDB_142078,IEDB_143253,IEDB_143794,IEDB_150899,IEDB_150939,IEDB_151531,IEDB_158550,IEDB_167188,IEDB_174332,IEDB_190606,IEDB_225177,IEDB_885823,SB_137,SB_165,SB_166,SB_173,SB_187,SB_195,SB_29,SB_30,SB_7,SB_88

Methods: 1H NMR, methylation, GC-MS, ESI-MS/MS, Smith degradation, MALDI-TOF MS, composition analysis, enzymatic digestion, extraction, HF treatment, HPTLC, RP-HPLC, adherence assay
Comments, role: proposed structure of T. vaginalis lipoglycan (TvLG) following digestion β-galactosidase and β-hexosaminidase.

Related record ID(s): 7364, 8364, 8366
NCBI Taxonomy refs (TaxIDs): 5722
Show glycosyltransferases

There is only one chemically distinct structure:

[*]O[C@@H]1[C@@H](O)[C@H](C)O[C@@H](O[C@@H]2[C@@H](O)[C@H](C)O[C@@H](O[C@@H]3[C@@H](O)[C@H](C)O[C@@H](O[C@@H]4[C@@H](O)[C@H](C)O[C@@H](O[C@@H]5[C@@H](O)[C@H](C)O[C@@H](O[C@@H]6[C@@H](O)[C@H](C)O[C@@H](O[C@@H]7[C@@H](O)[C@H](C)O[C@@H](O[C@@H]8[C@@H](O)[C@H](C)O[C@@H]([*])[C@@H]8O[C@@H]8O[C@H](CO)[C@H](O)[C@H](O[C@@H]9O[C@H](CO)[C@@H](O[C@@H]%10O[C@H](CO)[C@H](O[C@@H]%11O[C@@H](C)[C@H](O)[C@@H](O)[C@H]%11O[C@@H]%11OC[C@@H](O)[C@H](O)[C@H]%11O)[C@H](O[C@@H]%11O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%11NC(C)=O)[C@H]%10O)[C@H](O)[C@H]9NC(C)=O)[C@H]8O)[C@@H]7O[C@@H]7OC[C@@H](O)[C@H](O)[C@H]7O)[C@@H]6O[C@@H]6OC[C@@H](O)[C@H](O)[C@H]6O)[C@@H]5O[C@@H]5O[C@H](CO)[C@@H](O[C@@H]6O[C@H](CO)[C@H](O)[C@H](O[C@@H]7O[C@H](CO)[C@@H](O[C@@H]8O[C@H](CO)[C@H](O)[C@H](O[C@@H]9O[C@H](CO)[C@@H](O[C@@H]%10O[C@H](CO)[C@H](O[C@@H]%11O[C@@H](C)[C@H](O)[C@@H](O)[C@H]%11O[C@@H]%11OC[C@@H](O)[C@H](O)[C@H]%11O)[C@H](O[C@@H]%11O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%11NC(C)=O)[C@H]%10O)[C@H](O)[C@H]9NC(C)=O)[C@H]8O)[C@H](O)[C@H]7NC(C)=O)[C@H]6O)[C@H](O)[C@H]5NC(C)=O)[C@@H]4O[C@@H]4OC[C@@H](O[1*])[C@H](O)[C@H]4O)[C@@H]3O[C@@H]3O[C@H](CO)[C@@H](O)[C@H](O[C@@H]4O[C@H](CO)[C@H](O)[C@H](O[C@@H]5O[C@H](CO)[C@@H](O[C@@H]6O[C@H](CO)[C@H](O)[C@H](O[C@@H]7O[C@H](CO)[C@@H](O[C@@H]8O[C@H](CO)[C@H](O)[C@H](O[C@@H]9O[C@H](CO)[C@@H](O[C@@H]%10O[C@H](CO)[C@H](O[C@@H]%11O[C@@H](C)[C@H](O)[C@@H](O)[C@H]%11O[C@@H]%11OC[C@@H](O[1*])[C@H](O)[C@H]%11O)[C@H](O[C@@H]%11O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%11NC(C)=O)[C@H]%10O)[C@H](O)[C@H]9NC(C)=O)[C@H]8O)[C@H](O)[C@H]7NC(C)=O)[C@H]6O)[C@H](O)[C@H]5NC(C)=O)[C@H]4O)[C@H]3NC(C)=O)[C@@H]2O[C@@H]2OC[C@@H](O[1*])[C@H](O)[C@H]2O)[C@@H]1O[C@@H]1O[C@H](CO)[C@H](O)[C@H](O[C@@H]2O[C@H](CO)[C@@H](O[C@@H]3O[C@H](CO)[C@H](O[C@@H]4O[C@@H](C)[C@H](O)[C@@H](O)[C@H]4O[C@@H]4OC[C@@H](O)[C@H](O)[C@H]4O)[C@H](O[C@@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4NC(C)=O)[C@H]3O)[C@H](O)[C@H]2NC(C)=O)[C@H]1O

SVG MW SMILES 3D mol Ionize

R1 = SUG