Functional analysis of SleC from Clostridium difficile: An essential lytic transglycosylase involved in spore germination

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DOIResolve DOI: http://doi.org/10.1099/mic.0.072454-0
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TypeArticle
Journal titleMicrobiology (United Kingdom)
ISSN1350-0872
Volume160
IssuePART 1
Pages209216; # of pages: 8
Subjectbacterial protein; cellulase; glycosyltransferase; peptidoglycan; slec protein; unclassified drug; xylan endo 1,3 beta xylosidase; article; bioinformatics; catalysis; Clostridium; Clostridium difficile; controlled study; enzyme active site; enzyme activity; enzyme analysis; enzyme binding; nonhuman; priority journal; protein binding; spore germination
AbstractClostridium difficile is the most common cause of enteric disease and presents a major burden on healthcare systems globally due in part to the observed rapid rise in antibiotic resistance. The ability of C. difficile to form endospores is a key feature in the organism's pathogenesis and transmission, and contributes greatly to its resilient nature. Endospores are highly resistant to disinfection, allowing them to persist on hospital surfaces. In order for the organism to cause disease, the spores must germinate and revert to a vegetative form. While spore germination in Bacillus spp. is well understood, very little is known about this process in Clostridia. Here we report the characterization of SleC (CD0551) from C. difficile 630. Bioinformatic analysis of SleC indicated a multi-domained protein possessing a peptidoglycan-binding (PGB) domain, a SpoIID/LytB domain and an undefined N-terminal region. We have confirmed that SleC is an exo-acting lytic transglycosylase with the catalytic activity localized to the N-terminal region. Additionally, we have shown that both the N-terminal catalytic domain and the C-terminal PGB domain require muramyl-δ-lactam for substrate binding. As with carbohydrate-binding modules from cellulases and xylanases, the PGB domain may be responsible for increasing the processivity of SleC by concentrating the enzyme at the surface of the substrate. © 2014 SGM.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada (NRC-CNRC); Human Health Therapeutics (HHT-TSH)
Peer reviewedYes
NPARC number21270774
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Record identifierd07c10db-841d-4b52-b367-87ba8bf4b67a
Record created2014-02-17
Record modified2016-05-09
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