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Detailed Investigation of the Immunodominant Role of O-Antigen Stoichiometric O-Acetylation as Revealed by Chemical Synthesis, Immunochemistry, Solution Conformation and STD-NMR Spectroscopy for Shigella flexneri 3a
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2016 (English)In: Chemistry - A European Journal, ISSN 0947-6539, E-ISSN 1521-3765, Vol. 22, no 31, 10892-10911 p.Article in journal (Refereed) Published
Abstract [en]

Shigella flexneri 3a causes bacillary dysentery. Its O-antigen has the {2)-[alpha-d-Glcp-(1 -> 3)]-alpha-L-Rhap-(1 -> 2)-alpha-L-Rhap-( 1 -> 3)-[Ac -> 2]-alpha-L-Rhap-(1 ->)-[Ac -> 6](approximate to 40%)-beta-D-GlcpNAc-(1 ->} ([(E)AB(Ac)C(Ac)D]) repeating unit, and the non-Oacetylated equivalent defines S. flexneri X. Propyl hepta-, octa-, and decasaccharides sharing the (E') A'BAcCD(E) A sequence, and their non-O-acetylated analogues were synthesized from a fully protected BAcCD(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 2(C)-acetate dominated the recognition by monoclonal IgG and IgM antibodies and that the BAcCD 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.

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2016. Vol. 22, no 31, 10892-10911 p.
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URN: urn:nbn:se:su:diva-135902DOI: 10.1002/chem.201600567ISI: 000382885500028PubMedID: 27376496OAI: oai:DiVA.org:su-135902DiVA: diva2:1049792
Available from: 2016-11-25 Created: 2016-11-25 Last updated: 2016-11-25

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