A Fibrinogen-Binding Protein of Staphylococcus epidermidis
- 1 June 1998
- journal article
- Published by American Society for Microbiology in Infection and Immunity
- Vol. 66 (6), 2666-2673
- https://doi.org/10.1128/iai.66.6.2666-2673.1998
Abstract
The present study reports on fibrinogen (Fg) binding of Staphylococcus epidermidis. Adhesion of different S. epidermidis strains to immobilized Fg was found to vary significantly between different strains, and the component responsible was found to be proteinaceous in nature. To further characterize the Fg-binding activity, a shotgun phage display library covering the S. epidermidis chromosome was constructed. By affinity selection (panning) against immobilized Fg, a phagemid clone, pSEFG1, was isolated, which harbors an insert with an open reading frame of ∼1.7 kilobases. Results from binding and inhibition experiments demonstrated that the insert of pSEFG1 encodes a specific Fg-binding protein. Furthermore, affinity-purified protein encoded by pSEFG1 completely inhibited adhesion of S. epidermidis to immobilized Fg. By additional cloning and DNA sequence analyses, the complete gene, termed fbe, was found to consist of an open reading frame of 3,276 nucleotides encoding a protein, called Fbe, with a deduced molecular mass of ∼119 kDa. With a second phage display library made from another clinical isolate of S. epidermidis, it was possible to localize the Fg-binding region to a 331-amino-acid-long fragment. PCR analysis showed that the fbe gene was found in 40 of 43 clinical isolates of S. epidermidis. The overall organization of Fbe resembles those of other extracellular surface proteins of staphylococci and streptococci. Sequence comparisons with earlier known proteins revealed that this protein is related to an Fg-binding protein of Staphylococcus aureus called clumping factor.Keywords
This publication has 36 references indexed in Scilit:
- Characterization of coagulase-negative Staphylococci causing nosocomial infections in preterm infantsEuropean Journal of Clinical Microbiology & Infectious Diseases, 1995
- Identification of the ligand‐binding domain of the surface‐located fibrinogen receptor (clumping factor) of Staphylococcus aureusMolecular Microbiology, 1995
- Structure of the Cell Wall Anchor of Surface Proteins in Staphylococcus aureusScience, 1995
- Variation in the size of the repeat region of the fibrinogen receptor (clumping factor) of Staphylococcus aureus strainsMicrobiology, 1995
- Adhesion of coagulase-negative staphylococci and adsorption of plasma proteins to heparinized polymer surfacesBiomaterials, 1994
- Adhesion of staphylococci to chemically modified and native polymers, and the influence of preadsorbed fibronectin, vitronectin and fibrinogenBiomaterials, 1993
- Sorting of protein a to the staphylococcal cell wallCell, 1992
- Surface-immobilized polyethylene oxide for bacterial repellenceBiomaterials, 1992
- Isolation and Characterization of a Capsular Polysaccharide Adhesin from Staphylococcus epidermidisThe Journal of Infectious Diseases, 1988
- Optimal alignments in linear spaceBioinformatics, 1988