Three Streptococcus pneumoniae sialidases: Three different products

Guogang Xu, Milton Kiefel, Jennifer Wilson, Peter Andrew, Marco Oggioni, Garry Lindsay Taylor

Research output: Contribution to journalArticlepeer-review

94 Citations (Scopus)

Abstract

Streptococcus penumoniae is a major human pathogen responsible for respiratory tract infections, septicemia, and meningitis and continues to produce numerous cases of disease with relatively high mortalities. S. pneumoniae encodes up to three sialidases, NanA, NanB, and NanC, that have been implicated in pathogenesis and are potential drug targets. NanA has been shown to be a promiscuous sialidase, hydrolyzing the removal of Neu5Ac from a variety of glycoconjugates with retention of configuration at the anomeric center, as we confirm by NMR. NanB is an intramolecular trans-sialidase producing 2,7-anhydro-Neu5Ac selectively from α2,3-sialosides. Here, we show that the first product of NanC is 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en) that can be slowly hydrated by the enzyme to Neu5Ac. We propose that the three pneumococcal sialidases share a common catalytic mechanism up to the final product formation step, and speculate on the roles of the enzymes in the lifecycle of the bacterium
Original languageEnglish
Pages (from-to)1718-1721
JournalJournal of the American Chemical Society
Volume133
Issue number6
Early online date18 Jan 2011
DOIs
Publication statusPublished - 2011

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