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Role of Surface Protein SasG in Biofilm Formation by Staphylococcus aureus

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JournalJournal of Bacteriology
DatePublished - Nov 2010
Issue number21
Volume192
Number of pages11
Pages (from-to)5663-5673
Original languageEnglish

Abstract

The SasG surface protein of Staphylococcus aureus has been shown to promote the formation of biofilm. SasG comprises an N-terminal A domain and repeated B domains. Here we demonstrate that SasG is involved in the accumulation phase of biofilm, a process that requires a physiological concentration of Zn2+. The B domains, but not the A domain, are required. Purified recombinant B domain protein can form dimers in vitro in a Zn2+-dependent fashion. Furthermore, the protein can bind to cells that have B domains anchored to their surface and block biofilm formation. The full-length SasG protein exposed on the cell surface is processed within the B domains to a limited degree, resulting in cleaved proteins of various lengths being released into the supernatant. Some of the released molecules associate with the surface-exposed B domains that remain attached to the cell. Studies using inhibitors and mutants failed to identify any protease that could cause the observed cleavage within the B domains. Extensively purified recombinant B domain protein is very labile, and we propose that cleavage occurs spontaneously at labile peptide bonds and that this is necessary for biofilm formation.

    Research areas

  • POLYSACCHARIDE INTERCELLULAR ADHESIN, FIBRONECTIN-BINDING PROTEINS, MOLECULAR CHARACTERIZATION, ANTIBIOTIC-RESISTANCE, CLUMPING FACTOR, EPIDERMIDIS, FIBRINOGEN, ADHERENCE, VIRULENCE, AUTOLYSIN

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