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• W2133054195 abstract "Group B Streptococcus (GBS) is the leading cause of human neonatal sepsis and meningitis. The GBS capsular polysaccharide is a major virulence factor and the active principle of vaccines in phase II trials. All GBS capsules have a terminal alpha 2-3-linked sialic acid [N-acetylneuraminic acid (Neu5Ac)], which interferes with complement-mediated killing. We show here that some of the Neu5Ac residues of the GBS type III capsule are O-acetylated at carbon position 7, 8, or 9, a major modification evidently missed in previous studies. Data are consistent with initial O-acetylation at position 7, and subsequent migration of the O-acetyl ester at positions 8 and 9. O-acetylation was also present on several other GBS serotypes (Ia, Ib, II, V, and VI). Deletion of the CMP-Neu5Ac synthase gene neuA by precise, in-frame allelic replacement gave intracellular accumulation of O-acetylated Neu5Ac, whereas overexpression markedly decreased O-acetylation. Given the known GBS Neu5Ac biosynthesis pathway, these data indicate that O-acetylation occurs on free Neu5Ac, competing with the CMP-Neu5Ac synthase. O-acetylation often generates immunogenic epitopes on bacterial capsular polysaccharides and can modulate human alternate pathway complement activation. Thus, our discovery has important implications for GBS pathogenicity, immunogenicity, and vaccine design." @default.
• W2133054195 created "2016-06-24" @default.
• W2133054195 creator A5036413821 @default.
• W2133054195 creator A5039769184 @default.
• W2133054195 creator A5067852918 @default.
• W2133054195 date "2004-07-19" @default.
• W2133054195 modified "2023-09-26" @default.
• W2133054195 title "Discovery and characterization of sialic acid O-acetylation in group B <i>Streptococcus</i>" @default.
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• W2133054195 doi "https://doi.org/10.1073/pnas.0403010101" @default.
• W2133054195 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/503750" @default.
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• W2133054195 hasPublicationYear "2004" @default.
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