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J. Biol. Chem., Vol. 276, Issue 32, 29969-29978, August 10, 2001
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From the The fibrinogen-binding protein clumping factor B
(ClfB) of Staphylococcus aureus is present on the surface
of cells from the early exponential phase of growth in greater amounts
than on cells from late exponential phase and is barely detectable on
cells from stationary phase. Expression of a clfB-lacZ
fusion indicated that transcription stopped before the end of
exponential phase. Mutations in the global regulators agr
and sar had no effect on clfB transcription.
The loss of ClfB protein from cells in stationary phase was due to
expression ending before cells stopped growing, combined with shedding
of some of the protein into the growth medium and dilution of those
molecules remaining on the cell surface during the two to three cell
division events leading to stationary phase. Two forms of the protein
occurred on the cell surface, the smaller of which was generated by
loss of a domain from the N terminus. The proportion of the smaller
form increased as the cultures grew. The metalloprotease aureolysin was
shown to be responsible for cleavage of ClfB. Cleavage was inhibited by
EDTA and o-phenanthroline and did not occur in an
aureolysin-deficient mutant. Purified aureolysin promoted cleavage of
cell surface-located ClfB as well as the recombinant A domain of ClfB.
Cleavage was detected at two sites, one located between residues
Ser197 and Leu198 and the other between
Ala199 and Val200. The truncated form of ClfB
did not bind fibrinogen.
Loss of Clumping Factor B Fibrinogen Binding Activity by
Staphylococcus aureus Involves Cessation of Transcription,
Shedding and Cleavage by Metalloprotease*
,,¶
Microbiology Department, Moyne Institute for
Preventive Medicine, Trinity College, Dublin 2, Ireland and the
§ Microbiology Department, Institute of Molecular Biology,
Jagiellonian University, 31-120 Krakow, Poland
*
This work was supported by the Health Research Board of
Ireland and Wellcome Trust Grant 052320 (to T. J. F.) and by
Grant 6 P04A 083 20 from the Committee of Scientific Research (Komitet Badan Naukonych, Warsaw, Poland).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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