Abstract

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 beta chain of fibrinogen rather than the gamma chain, as in clumping factor A.

Published in

Infection and Immunity
1999, Volume: 67, number: 9, pages: 4525-4530
Publisher: AMER SOC MICROBIOLOGY

SLU Authors

• Guss, Bengt

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Microbiology
Immunology
Biochemistry and Molecular Biology


Publication identifier

DOI: https://doi.org/10.1128/IAI.67.9.4525-4530.1999

Permanent link to this page (URI)

https://res.slu.se/id/publ/79302