Cloning and characterization of two bistructural S-layer-RTX proteins from Campylobacter rectus

Braun, Martin; Kuhnert, Peter; Nicolet, Jacques; Burnens, André P.; Frey, Joachim (1999). Cloning and characterization of two bistructural S-layer-RTX proteins from Campylobacter rectus. Journal of bacteriology, 181(8), pp. 2501-2506. Washington, D.C.: American Society for Microbiology

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Campylobacter rectus is an important periodontal pathogen in humans. A surface-layer (S-layer) protein and a cytotoxic activity have been characterized and are thought to be its major virulence factors. The cytotoxic activity was suggested to be due to a pore-forming protein toxin belonging to the RTX (repeats in the structural toxins) family. In the present work, two closely related genes, csxA and csxB (for C. rectus S-layer and RTX protein) were cloned from C. rectus and characterized. The Csx proteins appear to be bifunctional and possess two structurally different domains. The N-terminal part shows similarity with S-layer protein, especially SapA and SapB of C. fetus and Crs of C. rectus. The C-terminal part comprising most of CsxA and CsxB is a domain with 48 and 59 glycine-rich canonical nonapeptide repeats, respectively, arranged in three blocks. Purified recombinant Csx peptides bind Ca2+. These are characteristic traits of RTX toxin proteins. The S-layer and RTX domains of Csx are separated by a proline-rich stretch of 48 amino acids. All C. rectus isolates studied contained copies of either the csxA or csxB gene or both; csx genes were absent from all other Campylobacter and Helicobacter species examined. Serum of a patient with acute gingivitis showed a strong reaction to recombinant Csx protein on immunoblots.

Item Type:

Journal Article (Original Article)

Division/Institute:

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

UniBE Contributor:

Kuhnert, Peter; Burnens, André and Frey, Joachim

Subjects:

600 Technology > 630 Agriculture
500 Science
500 Science > 570 Life sciences; biology

ISSN:

0021-9193

Publisher:

American Society for Microbiology

Language:

English

Submitter:

Peter Kuhnert-Ryser

Date Deposited:

30 Jan 2014 12:02

Last Modified:

13 Dec 2014 10:31

PubMed ID:

10198015

BORIS DOI:

10.7892/boris.39165

URI:

https://boris.unibe.ch/id/eprint/39165

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