期刊
JOURNAL OF BACTERIOLOGY
卷 192, 期 21, 页码 5663-5673出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.00628-10
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资金
- Science Foundation Ireland
- British Heart Foundation
- Health Research Board
- Fondazione CARIPLO [2009-3546]
- British Heart Foundation [FS/07/034/22969] Funding Source: researchfish
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 Zn(2+). The B domains, but not the A domain, are required. Purified recombinant B domain protein can form dimers in vitro in a Zn(2+)-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.
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