FEBS Letters
Volume 582, Issue 23 , Pages 3348-3352, 15 October 2008

Structural and functional studies of Streptococcus pneumoniae neuraminidase B: An intramolecular trans-sialidase

Edited by Hans Eklund

  • Heinz Gut

      Affiliations

    • MRC France, BM14 c/o ESRF, 6 rue Jules Horowitz, BP220, 38043 Grenoble, France
    • ,
  • Samantha J. King

      Affiliations

    • Center for Microbial Pathogenesis, The Research Institute at Nationwide Children’s Hospital, The Ohio State University College of Medicine, Columbus, OH 43205-2696, USA
    • ,
  • Martin A. Walsh

      Affiliations

    • MRC France, BM14 c/o ESRF, 6 rue Jules Horowitz, BP220, 38043 Grenoble, France
    • Corresponding Author InformationCorresponding author. Fax: +33 4 76 88 2380.

Received 29 July 2008; received in revised form 26 August 2008; accepted 26 August 2008. published online 05 September 2008.

Abstract 

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.

Abbreviations: NA, neuraminidase, IT-sialidase, intramolecular trans-sialidase, Neu5Ac, neuraminic acid

Keywords: Neuraminidase, NanB, Crystal structure, Intramolecular trans-sialidase, Streptococcus pneumoniae

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PII: S0014-5793(08)00713-8

doi:10.1016/j.febslet.2008.08.026

FEBS Letters
Volume 582, Issue 23 , Pages 3348-3352, 15 October 2008

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