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Infection and Immunity, September 1999, p. 4525-4530, Vol. 67, No. 9
Department of Immunology,
Received 2 February 1999/Returned for modification 6 April
1999/Accepted 17 June 1999
A gene encoding a fibrinogen binding protein from
Staphylococcus epidermidis was previously cloned, and the
nucleotide sequence was determined. A portion of the gene encompassing
the fibrinogen binding domain has now been subcloned in an
expression-fusion vector. The fusion protein can bind to fibrinogen in
a capture enzyme-linked immunosorbent assay and can be purified by
fibrinogen affinity chromatography. This protein can completely inhibit
the adherence of S. epidermidis to immobilized fibrinogen,
suggesting that the adherence of S. epidermidis to
fibrinogen is mainly due to this protein. Antibodies against this
fibrinogen binding protein were also found to efficiently block the
adherence of S. epidermidis to immobilized fibrinogen.
Despite homology with clumping factors A and B from S. aureus (cell surface-associated proteins binding to fibrinogen),
binding involved the
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Functional Studies of a Fibrinogen Binding Protein
from Staphylococcus epidermidis
chain of fibrinogen rather than the
chain,
as in clumping factor A.
*
Corresponding author. Mailing address: Department of
Immunology, Microbiology, Pathology, and Infectious Diseases,
Karolinska Institutet, Huddinge University Hospital, F82, S-141 86 Huddinge, Sweden. Phone: 46 8 58581169. Fax: 46 8 7113918. E-mail:
jan-ingmar.flock{at}impi.ki.se.
Infection and Immunity, September 1999, p. 4525-4530, Vol. 67, No. 9
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
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