Binding of Streptococcus mutans to extracellular matrix molecules and fibrinogen.
We have determined the ability of Streptococcus mutans cells to bind to extracellular matrix (ECM) molecules and fibrinogen. S. mutans cells were found to bind fibronectin, laminin, collagen type I, and fibrinogen. An isogenic S. mutans strain with a defect in the expression of the major surface protein of S. mutans, antigen I/II, possessed a reduced ability to bind fibronectin, collagen, and fibrinogen but not laminin, suggesting that antigen I/II contributes during pathological processes to the interaction of S. mutans cells with fibronectin, collagen type I, and fibrinogen.
Beg
Anjum M
AM
Department of Microbiology, Meharry Medical College, Nashville, TN 37208-3599, USA.
Jones
Micheala N
MN
Miller-Torbert
Tracey
T
Holt
Robert G
RG
D018829:Adhesins, Bacterial / Q000378:metabolism; D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000378:metabolism; D024042:Collagen Type I / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005340:Fibrinogen / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D007797:Laminin / Q000378:metabolism; D008562:Membrane Glycoproteins; D013295:Streptococcus mutans / Q000378:metabolism / Q000472:pathogenicity*
D018829:Adhesins, Bacterial; D001426:Bacterial Proteins; D024042:Collagen Type I; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D007797:Laminin; D008562:Membrane Glycoproteins; C055764:S-layer proteins; D005340:Fibrinogen