Binding of Streptococcus gordonii to extracellular matrix proteins.
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.
Giomarelli
Barbara
B
Laboratory of Molecular Microbiology and Biotechnology (LAMMB), Department of Molecular Biology, University of Siena, Siena, Italy.
Visai
Livia
L
Hijazi
Karolin
K
Rindi
Simonetta
S
Ponzio
Michela
M
Iannelli
Francesco
F
Speziale
Pietro
P
Pozzi
Gianni
G
D018829:Adhesins, Bacterial / Q000145:classification / Q000235:genetics*; D001422:Bacterial Adhesion / Q000502:physiology; D004797:Enzyme-Linked Immunosorbent Assay; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D009055:Mouth / Q000382:microbiology; D013291:Streptococcus / Q000235:genetics / Q000502:physiology*
D018829:Adhesins, Bacterial; D016326:Extracellular Matrix Proteins