Premium
The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes
Author(s) -
Gaillot Olivier,
Pellegrini Elisabeth,
Bregenholt Søren,
Nair Shamila,
Berche Patrick
Publication year - 2000
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 - 10.1046/j.1365-2958.2000.01773.x
Subject(s) - listeria monocytogenes , biology , virulence , microbiology and biotechnology , proteases , mutant , listeriolysin o , intracellular , complementation , pathogen , intracellular parasite , clpb , phagosome , listeria , bacteria , genetics , biochemistry , gene , enzyme
We identified the stress‐induced ClpP of Listeria monocytogenes and demonstrated its crucial role in intracellular survival of this pathogen. ClpP is a 21.6 kDa protein belonging to a family of proteases highly conserved in prokaryotes and eukaryotes. A clpP ‐deleted mutant enabled us to demonstrate that ClpP is involved in proteolysis and is required for growth under stress conditions. Intramacrophage survival of this mutant was strongly restricted, thus resulting in loss of virulence for the mouse. The activity of listeriolysin O, a major virulence factor implicated in bacterial escape from phagosomes of macrophages, was much reduced in the clpP mutant under stress conditions. Direct evidence for the role of ClpP in the intracellular parasitism was obtained by showing that virulence and haemolytic activity were fully restored by complementation of the mutant. These results suggest that ClpP is involved in the rapid adaptive response of intracellular pathogens during the infectious process.