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dc.contributor.authorSato, K
dc.contributor.authorSakai, E
dc.contributor.authorVeith, PD
dc.contributor.authorShoji, M
dc.contributor.authorKikuchi, Y
dc.contributor.authorYukitake, H
dc.contributor.authorOhara, N
dc.contributor.authorNaito, M
dc.contributor.authorOkamoto, K
dc.contributor.authorReynolds, EC
dc.contributor.authorNakayama, K
dc.date.available2014-05-21T19:40:52Z
dc.date.issued2005-03-11
dc.identifierpii: M413544200
dc.identifier.citationSato, 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.
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/11343/26624
dc.descriptionC1 - Journal Articles Refereed
dc.description.abstractThe 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.
dc.formatapplication/pdf
dc.languageEnglish
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.subjectAnalytical Biochemistry; Bacteriology ; Dentistry not elsewhere classified ; Prevention - Biologicals (e.g. Vaccines); Dental Health
dc.titleIdentification of a new membrane-associated protein that influences transport/maturation of gingipains and adhesins of Porphyromonas gingivalis
dc.typeJournal Article
dc.identifier.doi10.1074/jbc.M413544200
melbourne.peerreviewPeer Reviewed
melbourne.affiliationThe University of Melbourne
melbourne.affiliation.departmentDental Science
melbourne.source.titleJOURNAL OF BIOLOGICAL CHEMISTRY
melbourne.source.volume280
melbourne.source.issue10
melbourne.source.pages8668-8677
dc.research.coderfcd270101
dc.research.coderfcd270301
dc.research.coderfcd320899
dc.research.codeseo1998670401
dc.research.codeseo1998730214
melbourne.publicationid43439
melbourne.elementsid273368
melbourne.contributor.authorVeith, Paul
melbourne.contributor.authorReynolds, Eric
dc.identifier.eissn1083-351X
melbourne.accessrightsThis item is currently not available from this repository


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