@article{mbs:/content/journal/micro/10.1099/mic.0.038331-0, author = "Osbourne, Devon O. and Aruni, Wilson and Roy, Francis and Perry, Christopher and Sandberg, Lawrence and Muthiah, Arun and Fletcher, Hansel M.", title = "Role of vimA in cell surface biogenesis in Porphyromonas gingivalis", journal= "Microbiology", year = "2010", volume = "156", number = "7", pages = "2180-2193", doi = "https://doi.org/10.1099/mic.0.038331-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.038331-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "TLCK, N-α-p-tosyl-l-lysine chloromethyl ketone", keywords = "WTA, Triticum vulgaris lectin", keywords = "ConA, Concanavalin A", keywords = "DBA, Dolichos biflorus lectin", keywords = "MS, mass spectrometry", keywords = "ECA, Erythrina cristagalli lectin", keywords = "TSBKH, trypticase soy broth containing menadione and haemin", keywords = "ABA, Agaricus bisporus lectin", keywords = "BHI, brain–heart infusion", keywords = "LPS, lipopolysaccharide", keywords = "PAD, peptidyl arginine deiminase", keywords = "AFM, atomic force microscopy", keywords = "SBA, Glycine max lectin", keywords = "TEM, transmission electron microscopy", keywords = "LPA, Limulus polyphemus lectin", abstract = "The Porphyromonas gingivalis vimA gene has been previously shown to play a significant role in the biogenesis of gingipains. Further, in P. gingivalis FLL92, a vimA-defective mutant, there was increased auto-aggregation, suggesting alteration in membrane surface proteins. In order to determine the role of the VimA protein in cell surface biogenesis, the surface morphology of P. gingivalis FLL92 was further characterized. Transmission electron microscopy demonstrated abundant fimbrial appendages and a less well defined and irregular capsule in FLL92 compared with the wild-type. In addition, atomic force microscopy showed that the wild-type had a smoother surface compared with FLL92. Western blot analysis using anti-FimA antibodies showed a 41 kDa immunoreactive protein band in P. gingivalis FLL92 which was missing in the wild-type P. gingivalis W83 strain. There was increased sensitivity to globomycin and vancomycin in FLL92 compared with the wild-type. Outer membrane fractions from FLL92 had a modified lectin-binding profile. Furthermore, in contrast with the wild-type strain, nine proteins were missing from the outer membrane fraction of FLL92, while 20 proteins present in that fraction from FLL92 were missing in the wild-type strain. Taken together, these results suggest that the VimA protein affects capsular synthesis and fimbrial phenotypic expression, and plays a role in the glycosylation and anchorage of several surface proteins.", }