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Covalent attachment and Pro‐Pro endopeptidase (PPEP‐1)‐mediated release of Clostridium difficile cell surface proteins involved in adhesion
Author(s) -
Corver Jeroen,
Cordo’ Valentina,
van Leeuwen Hans C.,
Klychnikov Oleg I.,
Hensbergen Paul J.
Publication year - 2017
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13736
Subject(s) - biology , clostridium difficile , biofilm , microbiology and biotechnology , peptidoglycan , endopeptidase , adhesion , biochemistry , clostridium , cell adhesion , sortase , bacteria , cell , enzyme , chemistry , bacterial protein , genetics , organic chemistry , gene , antibiotics
Summary In the past decade, Clostridium difficile has emerged as an important gut pathogen. This anaerobic, Gram‐positive bacterium is the main cause of infectious nosocomial diarrhea. Whereas much is known about the mechanism through which the C. difficile toxins cause diarrhea, relatively little is known about the dynamics of adhesion and motility, which is mediated by cell surface proteins. This review will discuss the recent advances in our understanding of the sortase‐mediated covalent attachment of cell surface (adhesion) proteins to the peptidoglycan layer of C. difficile and their release through the action of a highly specific secreted metalloprotease (Pro‐Pro endopeptidase 1, PPEP‐1). Specific emphasis will be on a model in which PPEP‐1 and its substrates control the switch from a sessile to motile phenotype in C. difficile , and how this is regulated by the cyclic dinucleotide c‐di‐GMP (3′‐5′ cyclic dimeric guanosine monophosphate).