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Its O\u2010antigen has the {2)\u2010[\u03b1\u2010<jats:sc>d<\/jats:sc>\u2010Glc<jats:italic>p<\/jats:italic>\u2010(1\u21923)]\u2010\u03b1\u2010<jats:sc>l<\/jats:sc>\u2010Rha<jats:italic>p<\/jats:italic>\u2010(1\u21922)\u2010\u03b1\u2010<jats:sc>l<\/jats:sc>\u2010Rha<jats:italic>p<\/jats:italic>\u2010(1\u21923)\u2010[Ac\u21922]\u2010\u03b1\u2010<jats:sc>l<\/jats:sc>\u2010Rha<jats:italic>p<\/jats:italic>\u2010(1\u21923)\u2010[Ac\u21926]<jats:sub>\u224840\u2009%<\/jats:sub>\u2010\u03b2\u2010<jats:sc>d<\/jats:sc>\u2010Glc<jats:italic>p<\/jats:italic>NAc\u2010(1\u2192} ([(E)AB<jats:sub>Ac<\/jats:sub>C<jats:sub>Ac<\/jats:sub>D]) repeating unit, and the non\u2010<jats:italic>O<\/jats:italic>\u2010acetylated equivalent defines <jats:italic>S. flexneri<\/jats:italic>\u2005X. Propyl hepta\u2010, octa\u2010, and decasaccharides sharing the (E\u2032)A\u2032B<jats:sub>Ac<\/jats:sub>CD(E)A sequence, and their non\u2010<jats:italic>O<\/jats:italic>\u2010acetylated analogues were synthesized from a fully protected B<jats:sub>Ac<\/jats:sub>CD(E)A allyl glycoside. The stepwise introduction of orthogonally protected mono\u2010 and disaccharide imidate donors was followed by a two\u2010step deprotection process. Monoclonal antibody binding to twenty\u2010six <jats:italic>S. flexneri<\/jats:italic> types\u20053a and X di\u2010 to decasaccharides was studied by an inhibition enzyme\u2010linked immunosorbent assay (ELISA) and STD\u2010NMR spectroscopy. Epitope mapping revealed that the 2<jats:sub>C<\/jats:sub>\u2010acetate dominated the recognition by monoclonal IgG and IgM antibodies and that the B<jats:sub>Ac<\/jats:sub>CD segment was essential for binding. The glucosyl side chain contributed to a lesser extent, albeit increasingly with the chain length. 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