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  • Title: VimA-dependent modulation of the secretome in Porphyromonas gingivalis.
    Author: Osbourne D, Aruni AW, Dou Y, Perry C, Boskovic DS, Roy F, Fletcher HM.
    Journal: Mol Oral Microbiol; 2012 Dec; 27(6):420-35. PubMed ID: 23134608.
    Abstract:
    The VimA protein of Porphyromonas gingivalis is a multifunctional protein involved in cell surface biogenesis. To further determine if its acetyl coenzyme A (acetyl-CoA) transfer and putative sorting functions can affect the secretome, its role in peptidoglycan biogenesis and effects on the extracellular proteins of P. gingivalis FLL92, a vimA-defective mutant, were evaluated. There were structural and compositional differences in the peptidoglycan of P. gingivalis FLL92 compared with the wild-type strain. Sixty-eight proteins were present only in the extracellular fraction of FLL92. Fifteen proteins present in the extracellular fraction of the parent strain were missing in the vimA-defective mutant. These proteins had protein sorting characteristics that included a C-terminal motif with a common consensus Gly-Gly-CTERM pattern and a polar tail consisting of aromatic amino acid residues. These observations suggest that the VimA protein is likely involved in peptidoglycan synthesis, and corroborates our previous report, which suggests a role in protein sorting.
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