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      Aggregation substance-mediated adherence of Enterococcus faecalis to immobilized extracellular matrix proteins.

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          Abstract

          Aggregation substance (AS) of Enterococcus faecalis (E. faecalis), a sex pheromone plasmid encoded cell surface protein, mediates the formation of bacterial aggregates, thereby promoting plasmid transfer. The influence of pAD1-encoded AS, Asa1, on binding to immobilized extracellular matrix proteins was studied. The presence of AS increased enterococcal adherence to fibronectin more than eight-fold, to thrombospondin more than four-fold, to vitronectin more than three-fold, and to collagen type I more than two-fold (P<0.001). In contrast, binding to laminin and collagen type IV occurred independently of AS. Adherence of the constitutively AS expressing E. faecalis OG1X(pAM721) to immobilized fibronectin was found to be approximately five times higher than that of Staphylococcus aureus Cowan and approximately 30 times higher than that of Streptococcus bovis. Investigation of strains with various deletions within the structural gene of asa1 suggests that attachment to immobilized fibronectin is mainly mediated by amino acids within the variable region or by neighbouring residues. Thus, AS may promote adherence to injured epithelium and endothelium, where extracellular matrix proteins are exposed, thereby facilitating colonization and infection.

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          Author and article information

          Journal
          Microb. Pathog.
          Microbial pathogenesis
          0882-4010
          0882-4010
          Apr 2001
          : 30
          : 4
          Affiliations
          [1 ] Department of Medical Microbiology and Hygiene, University of Ulm, Ulm, D-89081, Germany. eva.rozdzinski@medizin.uni-ulm.de
          Article
          S0882-4010(00)90429-7
          10.1006/mpat.2000.0429
          11312614
          c4ea528d-ca23-4f16-ab7c-6e208c4b2ea0
          Copyright 2001 Academic Press.
          History

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