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 alpha2-3 linked sialic acid substrates. In addition, we show that NanB differs in its substrate specificity from the other pneumococcal neuraminidase NanA.
Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase.,Gut H, King SJ, Walsh MA FEBS Lett. 2008 Oct 15;582(23-24):3348-52. Epub 2008 Sep 5. PMID:18775704
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↑ Gut H, King SJ, Walsh MA. Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase. FEBS Lett. 2008 Oct 15;582(23-24):3348-52. Epub 2008 Sep 5. PMID:18775704 doi:10.1016/j.febslet.2008.08.026