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Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans ‐sialidase
Author(s) -
Gut Heinz,
King Samantha J.,
Walsh Martin A.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.08.026
Subject(s) - neuraminidase , streptococcus pneumoniae , sialidase , sialic acid , microbiology and biotechnology , neuraminic acid , biochemistry , virulence , enzyme , biology , chemistry , gene , antibiotics
The human pathogen Streptococcus pneumoniae expresses neuraminidase proteins that cleave sialic acids from complex carbohydrates. The pneumococcus genome encodes up to three neuraminidase proteins that have been shown to be important virulence factors. Here, we report the first structure of a neuraminidase from S. pneumoniae : the crystal structure of NanB in complex with its reaction product 2,7‐anhydro‐Neu5Ac. Our structural data, together with biochemical analysis, establish NanB as an intramolecular trans ‐sialidase with strict specificity towards α2‐3 linked sialic acid substrates. In addition, we show that NanB differs in its substrate specificity from the other pneumococcal neuraminidase NanA.