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Cited by 268

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The ClpP serine protease is essential for the intracellular parasitism and virulence of Listeria monocytogenes

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Gaillot, Olivier, Pellegrini, Elisabeth, Bregenholt, Søren, Nair, Shamila, Berche, Patrick·2000·Molecular Microbiology
DOI 10.1046/j.1365-2958.2000.01773.x
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Abstract

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.

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Metadata

Authors
Gaillot, O., Pellegrini, E., Bregenholt, S., Nair, S., & Berche, P.
Venue
Molecular Microbiology
Publisher
Wiley
Published
2000-03
Volume
35
Issue
6
Pages
1286-1294
ISSN
  • 0950-382X (ISSN-L)
  • 1365-2958
DOI
10.1046/j.1365-2958.2000.01773.x
OpenAlex
W1926946171
Cited by
268
References
0
FWCI
13.61
Type
journal article
Language
en
Open access
bronze

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