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J. Biol. Chem., Vol. 266, Issue 34, 23399-23406, 12, 1991
PW Park, DD Roberts, LE Grosso, WC Parks, J Rosenbloom, WR Abrams and RP Mecham
Many pathogenic bacteria specifically bind to components of the
extracellular matrix. In this study, we report the specific association of
Staphylococcus aureus with elastin, a major structural component of elastic
tissue. Competition assays in which the binding of radiolabeled
tropoelastin was inhibited by excess unlabeled elastin peptides, but not by
other proteins, established the specificity of the interaction. Kinetic
studies showed that tropoelastin binding to the bacteria was rapid and
saturable. Scatchard analysis of the equilibrium binding data indicated the
presence of a single class of high affinity binding sites (KD approximately
4-7 nM) with approximately 1000 sites per organism. Protease susceptibility
suggested that the elastin binding moiety on S. aureus was a protein, which
was confirmed by the isolation of a 25-kDa elastin-binding protein from S.
aureus extracts through affinity chromatography. Using a truncated form of
tropoelastin, the bacterial binding domain on elastin was mapped to a
30-kDa fragment at the amino end of the molecule. Although the precise
amino acid sequence recognized by the staphylococcal elastin receptor has
not been characterized, it is clearly different from the region of
tropoelastin that specifies binding to mammalian elastin receptors.
Binding of elastin to Staphylococcus aureus
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
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