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[39] Binding of extracellular matrix proteins by microbes

1995; Academic Press; Linguagem: Inglês

10.1016/s0076-6879(95)53041-x

1557-7988

Åsa Ljungh, Torkel Wadström,

Biochemical and Structural Characterization

This chapter discusses the binding of extracellular matrix (ECM) proteins by microbes. Proteins expose different microbial-binding domains when they are in soluble form and when they are immobilized in the ECM or on a biomaterial surface. This is confirmed by the finding that Yad A of Y. enterocolitica and P fimbriae of uropathogenic E. coli bind surface immobilized fibronectin (Fn) but not serum Fn. Binding of only immobilized or soluble forms of ECM proteins suggests that binding occurs to an epitope which is sensitive to conformational changes of the ECM molecules. Several of the identified ECM-binding structures on Staphylococcus aureus (S. aureus) and other bacteria are proteins, and hence the use of heat-killed bacteria may render false low or negative results. Proteases are produced by many microbial pathogens, and fibronectinolytic activity has been detected in strains of S. aureus, Staphylococcus epidermidis, Propionibacterium acnes, and a number of other anaerobic bacterial species. Binding of Fn by proteolytic bacterial strains may thus permit subsequent analysis of binding domains if the Fn is analyzed after proteolytic degradation in parallel. Most bacteria seem to express binding of ECM proteins during the exponential growth phase. The chapter also discusses ECM constituents, binding of soluble proteins and glycosaminoglycans, binding of immobilized proteins, binding of ECM proteins immobilized in tissue in vitro, and characterization of binding of ECM.