Journal of Bacteriology · 1986 · 130 citations · 31 references
Life SciencesMicrobiologyMolecular BiologyInnate ImmunityProtein-protein InteractionsStructural BiologyExtracellular MatrixPathogen AdhesionBacterial Adhesion MechanismsBacterial Adhesion RecognitionBacterial Surface ReceptorsCell Adhesion To CollagenCollagen-binding ProteinsNoncollagenous Matrix ProteinsNoncollagenous ProteinsScatchard Analysis
Collagen binds to a receptor protein present on the surfaces of Staphylococcus aureus cells. Binding of 125I-labeled type II collagen to its bacterial receptor is reversible, and Scatchard plot analysis indicates the presence of one class of receptor that occurs on an average of 3 X 10(4) copies per cell and binds type II collagen with a Kd of 10(-7) M. Studies on the specificity of collagen cell binding indicate that the receptor does not recognize noncollagenous proteins but binds all of the different collagen types tested (types I to VI). Furthermore, isolated collagen alpha chains and peptides generated by cyanogen bromide cleavage of type I collagen alpha chains are recognized by the receptor as indicated by the ability of these polypeptides to inhibit binding of 125I-labeled type II collagen to staphylococcal cells. Synthetic collagen analogs were tested as inhibitors of type II collagen binding to bacterial cells. The peptides (Pro-Gly-Pro)n, (Pro-Pro-Gly)10, and (Pro-OH-Pro-Gly)10 were recognized by the receptor, whereas the peptides (Pro-Ala-Gly)n and polyproline showed no inhibitory activity.
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Fibronectin binds to Staphylococcus aureus
Pentti Kuusela · Nature · 1978 · 459 citations
Nature of the Collagenous Protein in a Tumor Basement Membrane
Rupert Timpl, George R. Martin, Peter Brückner et al. · European Journal of Biochemistry · 1978 · 333 citations · Full text