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Identification of a novel zinc metalloprotease through a global analysis of clostridium difficile extracellular proteins

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Cafardi, Valeria, Biagini, Massimiliano, Martinelli, Manuele, Leuzzi, Rosanna, Rubino, Jeffrey T., Cantini, Francesca, Norais, Nathalie, Scarselli, Maria, Serruto, Davide and Unnikrishnan, Meera (2013) Identification of a novel zinc metalloprotease through a global analysis of clostridium difficile extracellular proteins. PLoS One, Volume 8 (Number 11). Article number e81306. doi:10.1371/journal.pone.0081306 ISSN 1932-6203.

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Official URL: http://dx.doi.org/10.1371/journal.pone.0081306

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Abstract

Clostridium difficile is a major cause of infectious diarrhea worldwide. Although the cell surface proteins are recognized to be important in clostridial pathogenesis, biological functions of only a few are known. Also, apart from the toxins, proteins exported by C. difficile into the extracellular milieu have been poorly studied. In order to identify novel extracellular factors of C. difficile, we analyzed bacterial culture supernatants prepared from clinical isolates, 630 and R20291, using liquid chromatography-tandem mass spectrometry. The majority of the proteins identified were non-canonical extracellular proteins. These could be largely classified into proteins associated to the cell wall (including CWPs and extracellular hydrolases), transporters and flagellar proteins. Seven unknown hypothetical proteins were also identified. One of these proteins, CD630_28300, shared sequence similarity with the anthrax lethal factor, a known zinc metallopeptidase. We demonstrated that CD630_28300 (named Zmp1) binds zinc and is able to cleave fibronectin and fibrinogen in vitro in a zinc-dependent manner. Using site-directed mutagenesis, we identified residues important in zinc binding and enzymatic activity. Furthermore, we demonstrated that Zmp1 destabilizes the fibronectin network produced by human fibroblasts. Thus, by analyzing the exoproteome of C. difficile, we identified a novel extracellular metalloprotease that may be important in key steps of clostridial pathogenesis.

Item Type: Journal Article
Subjects: R Medicine > R Medicine (General)
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences > Microbiology & Infection
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Clostridium difficile , Metalloproteinases, Zinc
Journal or Publication Title: PLoS One
Publisher: Public Library of Science
ISSN: 1932-6203
Official Date: 2013
Dates:
DateEvent
2013Published
Volume: Volume 8
Number: Number 11
Page Range: Article number e81306
DOI: 10.1371/journal.pone.0081306
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access (Creative Commons)
Date of first compliant deposit: 26 December 2015
Date of first compliant Open Access: 26 December 2015

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