Email updates

Keep up to date with the latest news and content from Veterinary Research and BioMed Central.

Open Access Research

Genetic and functional characterization of the NanA sialidase from Clostridium chauvoei

Edy M Vilei1*, Anders Johansson12, Yvonne Schlatter1, Keith Redhead3 and Joachim Frey1

Author Affiliations

1 Institute of Veterinary Bacteriology, Vetsuisse Faculty, University of Bern, Bern, Switzerland

2 National Food Administration, Uppsala, Sweden

3 Intervet/Schering-Plough Animal Health, Milton Keynes, UK

For all author emails, please log on.

Veterinary Research 2011, 42:2  doi:10.1186/1297-9716-42-2

Published: 11 January 2011

Abstract

Clostridium chauvoei is the causative agent of blackleg, a wide spread serious infection of cattle and sheep with high mortality. In this study we have analyzed the sialidase activity of the NanA protein of C. chauvoei and cloned the sialidase gene nanA. Sialidase is encoded as a precursor protein of 722 amino acids with a 26 amino acid signal peptide. The mature sialidase has a calculated molecular mass of 81 kDa and contains the carbohydrate binding module 32 (CBM32, or F5/8 type C domain), the sialic acid binding module CBM40 and the enzymatically active sialidase domain found in all pro- and eukaryotic sialidases. Sialidase activity does not require the CBM32 domain. The NanA protein is secreted by C. chauvoei as a dimer. The nanA gene was found to be conserved and sialidase activity was found in C. chauvoei strains isolated over a period of 50 years from various geographical locations. Antiserum directed against a recombinant 40 kDa peptide containing CBM40 and part of the enzymatically active domain of NanA neutralized the secreted sialidase activity of all C. chauvoei strains tested.