Genetic and functional characterization of the NanA sialidase from Clostridium chauvoei

Vilei, E.M.; Johansson, A.; Schlatter, Y.; Redhead, K.; Frey, J. (2011). Genetic and functional characterization of the NanA sialidase from Clostridium chauvoei. Veterinary research, 42(1), p. 2. Paris: Editions scientifiques Elsevier 10.1186/1297-9716-42-2

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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.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Infectious Diseases and Pathobiology (DIP) > Institute of Veterinary Bacteriology

UniBE Contributor:

Vilei, Edi, Schlatter, Yvonne, Frey, Joachim

ISSN:

0928-4249

Publisher:

Editions scientifiques Elsevier

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:31

Last Modified:

05 Dec 2022 14:10

Publisher DOI:

10.1186/1297-9716-42-2

Web of Science ID:

000290659000002

URI:

https://boris.unibe.ch/id/eprint/12138 (FactScience: 218426)

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