Open AccessVitronectin and type‐I collagen binding by Staphylococcus aureus and coagulase‐negative staphylococci
Author(s) -
Paulsson M.,
Wadström T.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb03479.x
Subject(s) - vitronectin , coagulase , staphylococcus aureus , chemistry , staphylococcus haemolyticus , protease , trypsin , biochemistry , binding protein , microbiology and biotechnology , binding site , staphylococcus , biology , integrin , receptor , enzyme , bacteria , gene , genetics
Binding of 125 I‐labelled type‐I collagen and 125 I‐labelled vitronectin (human serum spreading factor or S‐protein) was studied using Staphylococcus aureus and coagulase‐negative staphylococci of different species. Binding of collagen and vitronectin was time dependent for S. aureus ISP 546, and S. haemolyticus E 2498/86. Co‐operative binding of vitronectin and collagen by staphylococcal cells was demonstrated. Binding to S. haemolyticus E 2498/86 was more rapid and was enhanced in vitronectin/collagen mixtures than for either protein separately. Furthermore, pre‐incubation of staphylococcal cells with unlabelled collagen enhanced vitronectin binding. When cells of S. haemolyticus E 2498/86 were treated with pronase E, proteinase K, subtilopeptidase A or trypsin, vitronectin‐binding was decreased by 50% or more, whereas collagen‐binding was protease resistant. For the strains of S. aureus tested, both vitronectin and collagen binding were found to be protease sensitive. Type‐I collagen peptides inhibited collagen‐binding to S. haemolyticus E 2498/86, whereas vitronectin‐binding was not affected perhaps indicating different receptors for these proteins. The binding of both collagen and vitronectin was shown to be reversible, since bound 125 I‐collagen and 125 I‐vitronectin were displaced after adding excess of the homologous protein.