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Binding of Streptococcus gordonii to extracellular matrix proteins
Author(s) -
Giomarelli Barbara,
Visai Livia,
Hijazi Karolin,
Rindi Simonetta,
Ponzio Michela,
Iannelli Francesco,
Speziale Pietro,
Pozzi Gianni
Publication year - 2006
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.1574-6968.2006.00479.x
Subject(s) - streptococcus gordonii , mutant , fibronectin , extracellular matrix , biochemistry , chemistry , binding site , extracellular , plasma protein binding , biology , microbiology and biotechnology , gene , streptococcaceae , antibiotics
Knock‐out mutants of Streptococcus gordonii Challis were constructed and assayed for binding to extracellular matrix proteins (EMPs) by enzyme‐linked immunosorbent assay (ELISA). It was shown that (i) the mutant lacking the cell wall polysaccharide receptor could no longer bind type I and type II collagen, (ii) the mutant lacking the fibronectin‐binding proteins CshA and FbpA was also strongly impaired in collagen binding and (iii) the mutant lacking the methionine sulfoxide reductase MsrA was significantly impaired in fibronectin binding. Our results indicate that binding to EMPs by S. gordonii is a multifactorial process controlled by genes located at three different chromosomal sites.

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