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    Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis

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    Author
    Sato, K; Sakai, E; Veith, PD; Shoji, M; Kikuchi, Y; Yukitake, H; Ohara, N; Naito, M; Okamoto, K; Reynolds, EC; ...
    Date
    2005-03-11
    Source Title
    Journal of Biological Chemistry
    Publisher
    AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
    University of Melbourne Author/s
    Veith, Paul; Reynolds, Eric
    Affiliation
    Dental Science
    Metadata
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    Document Type
    Journal Article
    Citations
    Sato, K., Sakai, E., Veith, P. D., Shoji, M., Kikuchi, Y., Yukitake, H., Ohara, N., Naito, M., Okamoto, K., Reynolds, E. C. & Nakayama, K. (2005). Identification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis. JOURNAL OF BIOLOGICAL CHEMISTRY, 280 (10), pp.8668-8677. https://doi.org/10.1074/jbc.M413544200.
    Access Status
    This item is currently not available from this repository
    URI
    http://hdl.handle.net/11343/26624
    DOI
    10.1074/jbc.M413544200
    Description

    C1 - Journal Articles Refereed

    Abstract
    The dual membrane envelopes of Gram-negative bacteria provide two barriers of unlike nature that regulate the transport of molecules into and out of organisms. Organisms have developed several systems for transport across the inner and outer membranes. The Gram-negative periodontopathogenic bacterium Porphyromonas gingivalis produces proteinase and adhesin complexes, gingipains/adhesins, on the cell surface and in the extracellular milieu as one of the major virulence factors. Gingipains and/or adhesins are encoded by kgp, rgpA, rgpB, and hagA on the chromosome. In this study, we isolated a P. gingivalis mutant (porT), which showed very weak activities of gingipains in the cell lysates and culture supernatants. Subcellular fractionation and immunoblot analysis demonstrated that precursor forms of gingipains and adhesins were accumulated in the periplasmic space of the porT mutant cells. Peptide mass fingerprinting and N-terminal amino acid sequencing of the precursor proteins and the kgp'-'rgpB chimera gene product in the porT mutant indicated that these proteins lacked the signal peptide regions, consistent with their accumulation in the periplasm. The PorT protein seemed to be membrane-associated and exposed to the periplasmic space, as revealed by subcellular fractionation and immunoblot analysis using anti-PorT antiserum. These results suggest that the membrane-associated protein PorT is essential for transport of the kgp, rgpA, rgpB, and hagA gene products across the outer membrane from the periplasm to the cell surface, where they are processed and matured.
    Keywords
    Analytical Biochemistry; Bacteriology ; Dentistry not elsewhere classified ; Prevention - Biologicals (e.g. Vaccines); Dental Health

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