Volume 27, Issue 6 p. 420-435

VimA–dependent modulation of the secretome in Porphyromonas gingivalis

D. Osbourne,

Division of Microbiology & Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda CA, USA

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A. Wilson Aruni,

Division of Microbiology & Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda CA, USA

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Y. Dou,

Division of Microbiology & Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda CA, USA

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C. Perry,

Division of Biochemistry, School of Medicine, Loma Linda University, Loma Linda CA, USA

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D.S. Boskovic,

Division of Biochemistry, School of Medicine, Loma Linda University, Loma Linda CA, USA

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F. Roy,

Division of Microbiology & Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda CA, USA

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H. M. Fletcher,

Division of Microbiology & Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda CA, USA

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First published: 12 July 2012
Citations: 6
Hansel M. Fletcher, Division of Microbiology & Molecular Genetics, School of Medicine, Loma Linda University, Loma Linda, CA 92350, USA Tel.: +1 909 558 4472; fax: +1 909 558 4035; E-mail: hfletcher@llu.edu

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.

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