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- W2154686541 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." @default.
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- W2154686541 date "2012-08-09" @default.
- W2154686541 modified "2023-09-26" @default.
- W2154686541 title "VimA-dependent modulation of the secretome in<i>Porphyromonas gingivalis</i>" @default.
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- W2154686541 doi "https://doi.org/10.1111/j.2041-1014.2012.00661.x" @default.
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