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VimA–dependent modulation of the secretome in Porphyromonas gingivalis
Author(s) -
Osbourne D.,
Wilson Aruni A.,
Dou Y.,
Perry C.,
Boskovic D.S.,
Roy F.,
Fletcher H. M.
Publication year - 2012
Publication title -
molecular oral microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 77
eISSN - 2041-1014
pISSN - 2041-1006
DOI - 10.1111/j.2041-1014.2012.00661.x
Subject(s) - biogenesis , peptidoglycan , porphyromonas gingivalis , extracellular , microbiology and biotechnology , biology , mutant , protein targeting , biochemistry , chemistry , membrane protein , bacteria , cell wall , genetics , gene , membrane
Summary 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.