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Infection and Immunity, December 2000, p. 7061-7068, Vol. 68, No. 12
Unité de Physiopathologie
Moléculaire des Infections Microbiennes, INSERM U411,
Faculté de Médecine Necker, 75730 Paris Cedex 15, France
Received 3 July 2000/Returned for modification 16 August
2000/Accepted 18 September 2000
We studied the role of two members of the 100-kDa heat shock
protein family, the ClpC and ClpE ATPases, in cell adhesion
and invasion of the intracellular pathogen Listeria
monocytogenes. During the early phase of infection, a
clpC mutant failed to disseminate to hepatocytes in the
livers of infected mice whereas the invasive capacity of a
clpE mutant remained unchanged. This was confirmed by a
confocal microscopy study on infected cultured hepatocyte and
epithelial cell lines, showing a strong reduction of cell invasion only
by the clpC mutant. Western blot analysis with specific antisera showed that the absence of ClpC, but not that of ClpE, reduced
expression of the virulence factors InlA, InlB, and ActA. ClpC-dependent modulation of these factors occurs at the
transcriptional level with a reduction in the transcription of
inlA, inlB, and actA in the
clpC mutant, in contrast to the clpE mutant.
This work provides the first evidence that, in addition to promoting escape from the phagosomes, ClpC is required for adhesion and invasion
and modulates the expression of InlA, InlB, and ActA, further
supporting the major role of the Clp chaperones in the virulence of
intracellular pathogens.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
ClpC ATPase Is Required for Cell Adhesion
and Invasion of Listeria monocytogenes
*
Corresponding author. Mailing address: Unité de
Physiopathologie Moléculaire des Infections Microbiennes, INSERM
U411, Faculté de Médecine Necker, 156, rue de Vaugirard,
75730 Paris Cedex 15, France. Phone: 33 1 40 61 53 73. Fax: 33 1 40 61 55 92. E-mail: berche{at}necker.fr.
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