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• W2473278314 startingPage "10892" @default.
• W2473278314 abstract "Abstract Shigella flexneri 3a causes bacillary dysentery. Its O‐antigen has the {2)‐[α‐ d ‐Glc p ‐(1→3)]‐α‐ l ‐Rha p ‐(1→2)‐α‐ l ‐Rha p ‐(1→3)‐[Ac→2]‐α‐ l ‐Rha p ‐(1→3)‐[Ac→6] ≈40 % ‐β‐ d ‐Glc p NAc‐(1→} ([(E)AB Ac C Ac D]) repeating unit, and the non‐ O ‐acetylated equivalent defines S. flexneri X. Propyl hepta‐, octa‐, and decasaccharides sharing the (E′)A′B Ac CD(E)A sequence, and their non‐ O ‐acetylated analogues were synthesized from a fully protected B Ac 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 2 C ‐acetate dominated the recognition by monoclonal IgG and IgM antibodies and that the B Ac 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." @default.
• W2473278314 created "2016-07-22" @default.
• W2473278314 creator A5032855763 @default.
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• W2473278314 date "2016-07-04" @default.
• W2473278314 modified "2023-10-17" @default.
• W2473278314 title "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<i>Shigella flexneri</i> 3a" @default.
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