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Journal of Bacteriology, July 2000, p. 3955-3964, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
A New Two-Component Regulatory System Involved in Adhesion,
Autolysis, and Extracellular Proteolytic Activity of
Staphylococcus aureus
Bénédicte
Fournier1,2,* and
David C.
Hooper1
Infectious Disease Division and Medical
Services, Massachusetts General Hospital, Harvard Medical School,
Boston, Massachusetts 02114-2696,1 and
Unité de Biochimie Microbienne, CNRS URA 1300, Institut Pasteur, 75724 Paris Cedex 15, France2
Received 7 February 2000/Accepted 27 April 2000
A transposition mutant of Staphylococcus aureus was
selected from the parent strain MT23142, a derivative of strain 8325. The site of transposition was near the 5' terminus of the gene arlS. ArlS exhibits strong similarities with histidine
protein kinases. Sequence analysis suggested that arlS
forms an operon with upstream gene arlR. The predicted
product of arlR is a member of the OmpR-PhoB family of
response regulators. The arlS mutant formed a biofilm on a
polystyrene surface unlike the parent strain and the complemented
mutant. Biofilm formation was associated with increased primary
adherence to polystyrene, whereas cellular adhesion was only slightly
decreased. In addition, the arlS mutant exhibited increased
autolysis and altered peptidoglycan hydrolase activity compared to the
parental strain and to the complemented mutant. As it has been shown
for coagulase-negative staphylococci that some autolysins are able to
bind polymer surfaces, these data suggest that the two-component
regulatory system ArlS-ArlR may control attachment to polymer surfaces
by affecting secreted peptidoglycan hydrolase activity. Finally, the
arlS mutant showed a dramatic decrease of extracellular
proteolytic activity, including serine protease activity, in comparison
to the wild-type strain and the complemented mutant, and cells grown in
the presence of phenylmethylsulfonyl fluoride (a serine protease
inhibitor) showed an increased autolysin activity. Since the locus
arlR-arlS strikingly modifies extracellular proteolytic
activity, this locus might also be involved in the virulence of
S. aureus.
*
Corresponding author. Mailing address: Unité de
Biochimie Microbienne, Institut Pasteur, 25, rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: (33) 1 45 68 88 09. Fax: (33) 1 45 68 89 38. E-mail: bfournie{at}pasteur.fr.
Journal of Bacteriology, July 2000, p. 3955-3964, Vol. 182, No. 14
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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