EXTRACELLULAR-MATRIX PROTEINS (FIBRONECTIN, LAMININ, AND TYPE-IV COLLAGEN) BIND AND AGGREGATE BACTERIA

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  • 1 January 1985
    • journal article
    • research article
    • Vol. 120  (1) , 13-21
Abstract
The normal microbial colonization of sites in the body''s tissues by certain bacteria requires that the bacteria first bind to extracellular secreted constituents, cell-surface membranes or cell matrixes. This study examines 2 interactions of a variety of bacteria with the cell matrix noncollagenous proteins fibronectin and laminin and with basement membrane (Type IV) collagen. Adherence of bacteria to matrix proteins coated on tissue culture wells was examined with the use of radiolabeled bacteria. Staphylococcus aureus, Streptococcus pyogenes and Streptococcus sanguis bound well to fibronectin, laminin and Type IV collagen, whereas a variety of gramnegative organisms did not bind. The interaction of soluble laminin, fibronectin and Type IV collagen with bacteria was monitored by nephelometry with the use of a platelet aggregometer. S. aureus aggregated in response to fibronectin, laminin or Type IV collagen. In contrast, gram-negative organims did not aggregate with these proteins. Fibronectin, laminin and Type IV collagen apparently can bind and aggregate certain gram-positive bacteria, and this binding is dependent on the surface characteristics of the organism. These adhesion molecules may play a role in the normal colonization of sites by microorganisms and in invasion during infections.