Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: bacillary dysentery (shigellosis) [ICD11:
1A02 
, ICD11:
SA56 , ICD11:
XN7HG ];
infection due to Shigella flexneri [ICD11:
XN7Y2 ]
NCBI PubMed ID: 27376496Publication DOI: 10.1002/chem.201600567Journal NLM ID: 9513783Publisher: Weinheim: VCH Verlagsgesellschaft/Verlag I
Correspondence: laurence.mulard
pasteur.fr; jjbarbero
cicbiogune.es
Institutions: Dept. of Organic Chemistry, Arrhenius Laboratory, Stockholm University, 10691, Stockholm, Sweden, Institut Pasteur, Unite de Pathogenie Microbienne Moleculaire, 28 rue du Dr. Roux, 75015, Paris, France, INSERM U1202, Institut Pasteur, 75015, Paris, France, Chemical and Physical Biology, Centro de Investigaciones Biologicas, CSIC, Ramiro de Maeztu 9, 28040, Madrid, Spain, Molecular Recognition & Host-Pathogen Interactions Program, CIC bioGUNE, Bizkaia Technological Park, Building 801A, 48160, Derio, Spain, Ikerbasque, Basque Foundation for Science, Maria Lopez de Haro 3, 48013, Bilbao, Spain, Institut Pasteur, Unite de Chimie des Biomolecules, 28 rue du Dr. Roux, 75724, Paris Cedex 15, France, CNRS UMR 3523, Institut Pasteur, 75015, Paris, France
Shigella flexneri 3a causes bacillary dysentery. Its O-antigen has the {2)-[α-d-Glcp-(1→3)]-α-l-Rhap-(1→2)-α-l-Rhap-(1→3)-[Ac→2]-alp ha-l-Rhap-(1→3)-[Ac→6] approximately 40 % -β-d-GlcpNAc-(1→} ([(E)ABAc CAc D]) repeating unit, and the non-O-acetylated equivalent defines S. flexneri X. Propyl hepta-, octa-, and decasaccharides sharing the (E')A'BAc CD(E)A sequence, and their non-O-acetylated analogues were synthesized from a fully protected BAc CD(E)A allyl glycoside. The stepwise introduction of orthogonally protected mono- and disaccharide imidate donors was followed by a two-step deprotection process. Monoclonal antibody binding to twenty-six S. flexneri types 3a and X di- to decasaccharides was studied by an inhibition enzyme-linked immunosorbent assay (ELISA) and STD-NMR spectroscopy. Epitope mapping revealed that the 2C -acetate dominated the recognition by monoclonal IgG and IgM antibodies and that the BAc CD segment was essential for binding. The glucosyl side chain contributed to a lesser extent, albeit increasingly with the chain length. Moreover, tr-NOESY analysis also showed interaction but did not reveal any meaningful conformational change upon antibody binding.
carbohydrates, antibodies, NMR spectroscopy, glycosylation, epitope specificity
Structure type: polymer chemical repeating unit
Location inside paper: abstract, p.10893, fig.1, structure II
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125613,IEDB_125614,IEDB_127514,IEDB_133752,IEDB_133753,IEDB_133754,IEDB_135813,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_141815,IEDB_141816,IEDB_142488,IEDB_143253,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_153213,IEDB_158539,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, TLC, ELISA, conformation analysis, chemical synthesis, chemical methods, MD simulations, serological methods, STD NMR, glycosylation, immunochemical methods
3D data: 3D data
Related record ID(s): 11357
NCBI Taxonomy refs (TaxIDs): 623Reference(s) to other database(s): GTC:G25789RV, GlycomeDB:
33490
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
report error