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The ClpC ATPase of Listeria monocytogenes is a general stress protein required for virulence and promoting early bacterial escape from the phagosome of macrophages by Corinne Rouquette; Chantal De Chastellier; Shamila Nair; Patrick Berche is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Under stress conditions, the facultative intracellular pathogen __Listeria monocytogenes__ produces a ClpC ATPase, which is a general stress protein encoded by __clpC__ and belonging to the HSP‐100/Clp family. A ClpC‐deficient mutant was obtained by gene disruption in strain LO28, which became highly susceptible to stress conditions __in vitro__. Intracellular growth of this mutant was restricted within macrophages, one of the major target cells of __L__. __monocytogenes__, during the infectious process. A quantitative electron microscope study showed that, contrary to wild‐type bacteria that rapidly gain access to the cytoplasm of macrophages, mutant bacteria remained confined to membrane‐bound phagosomes. Only a few mutant bacteria disrupted the phagosome membrane after 4 h of incubation, then polymerized actin filaments and multiplied within the cytoplasm. The ClpC ATPase, therefore, promotes early bacterial escape from the phagosome of macrophages, thus enhancing intracellular survival. The ClpC ATPase was produced __in vivo__ during experimental infection by wild‐type bacteria. The virulence of the ClpC‐deficient mutant was severely attenuated in mice, with a three‐log decreas

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Author

Corinne Rouquette; Chantal De Chastellier; Shamila Nair; Patrick Berche

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0950-382X)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)