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• W1966776870 abstract "We have identified a gene for the addition of N‐ acetylneuraminic acid (Neu5Ac) in an α‐2,3‐linkage to a lactosyl acceptor moiety of the lipopolysaccharide (LPS) of the human pathogen Haemophilus influenza e. The gene is one that was identified previously as a phase‐variable gene known as lic3A . Extracts of H. influenzae , as well as recombinant Escherichia coli strains producing Lic3A, demonstrate sialyltransferase activity in assays using synthetic fluorescent acceptors with a terminal galactosyl, lactosyl or N‐ acetyl‐lactosaminyl moiety. In the RM118 strain of H. influenzae , Lic3A activity is modulated by the action of another phase‐variable glycosyltransferase, LgtC, which competes for the same lactosyl acceptor moiety. Structural analysis of LPS from a RM118: lgtC mutant and the non‐typeable strain 486 using mass spectrometry and nuclear magnetic resonance (NMR) spectroscopy confirmed that the major sialylated species has a sialyl‐α‐(2–3)‐lactosyl extension off the distal heptose. This sialylated glycoform was absent in strains containing a lic3A gene disruption. Low amounts of sialylated higher molecular mass glycoforms were present in RM118: lgtC lic3A , indicating the presence of a second sialyltransferase. Lic3A mutants of H. influenzae strains show reduced resistance to the killing effects of normal human serum. Lic3A , encoding an α‐2,3‐sialyltransferase activity, is the first reported phase‐variable sialyltransferase gene." @default.
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• W1966776870 date "2001-01-01" @default.
• W1966776870 modified "2023-10-18" @default.
• W1966776870 title "Identification of a lipopolysaccharide alpha-2,3-sialyltransferase from Haemophilus influenzae" @default.
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• W1966776870 doi "https://doi.org/10.1046/j.1365-2958.2001.02204.x" @default.
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