Open AccessSeveral regions of the repeat domain of the Staphylococcus caprae autolysin, AtlC, are involved in fibronectin binding
Author(s) -
Allignet Jeanine,
England Patrick,
Old Iain,
Solh Névine
Publication year - 2002
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.1574-6968.2002.tb11305.x
Subject(s) - autolysin , fibronectin , binding domain , microbiology and biotechnology , binding site , biology , chemistry , biochemistry , enzyme , extracellular matrix , peptidoglycan
The autolysin AtlC is the only known fibronectin‐binding protein in Staphylococcus caprae strain 96007. The fibronectin‐binding domain of AtlC consists of three repeats (AtlCR 1 R 2 R 3 ), which are located between the two enzymatic domains. The AtlCR 1 R 2 R 3 domain and the AtlCR 1 R 2 and AtlCR 3 subdomains were expressed separately as His 6 ‐tagged proteins. In Western affinity blots, only AtlCR 1 R 2 R 3 and AtlCR 3 but not AtlCR 1 R 2 appeared to recognise fibronectin; however, in ELISA and Biacore experiments, all three bound fibronectin. The interaction between AtlCR 1 R 2 R 3 and fibronectin is multivalent and involves high‐ and low‐affinity sites that are present in a 2:1 ratio. These distinct classes of binding sites may be situated on either or on both ligands.