Affiliation:
1. School of Biological Sciences, Royal Holloway, University of London, Egham, Surrey TW20 0EX, United Kingdom
2. Laboratoire de Microbiologie, UMR5248 CNRS-Université ENITA de Bordeaux, 1, cours du Général de Gaulle, CS 40201, 33175 Gradignan, France
Abstract
ABSTRACT
Clostridium difficile
is an important human pathogen and one where the primary cause of disease is due to the transmission of spores. We have investigated the proteins found in the outer coat layers of
C. difficile
spores of pathogenic strain 630 (CD630). Five coat proteins, CotA, CotB, CotCB, CotD, and CotE, were shown to be expressed on the outer coat layers of the spore. We demonstrate that purified spores carry catalase, peroxiredoxin, and chitinase activity and that this activity correlates with the predicted functions of three spore coat proteins identified here, CotCB, CotD, and CotE. CotCB and CotD are putative manganese catalases, and CotE is a novel bifunctional protein with peroxiredoxin activity at its amino terminus and chitinase activity at its carboxy terminus. These enzymes could play an important role in coat assembly by polymerizing protein monomers in the coat. CotE, in addition to a role in macromolecular degradation, could play an important role in inflammation, and this may be of direct relevance to the development of the gastrointestinal symptoms that accompany
C. difficile
infection. Although specific enzyme activity has not yet been assigned to the proteins identified here, this work provides the first detailed study of the
C. difficile
spore coat.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
99 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献