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Article: Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola

TitleCytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola
Authors
Issue Date1998
PublisherAmerican Society for Microbiology.
Citation
Infection And Immunity, 1998, v. 66 n. 5, p. 1869-1877 How to Cite?
AbstractProminent antigens of Treponema denticola have been suggested to be mediators of the cytopathic effects typically seen in periodontal disease. In the present study of the T. denticola major surface protein (Msp) and the surface-expressed chymotrypsinlike protease complex (CTLP), we characterized the ability of these proteins to adhere to and lyse epithelial cells. Msp and CTLP were closely associated in spirochete outer membranes. Purified Msp, both native and recombinant, and CTLP bound to glutaraldehyde-fixed periodontal ligament epithelial cells. Adherence of Msp was partially blocked by specific antibodies. Adherence of CTLP was partially blocked by serine protease inhibitors and was further inhibited by specific antibodies. Both native Msp and CTLP were cytotoxic toward periodontal ligament epithelial cells, and their cytotoxicity was inhibited by the same treatments that inhibited adherence. Msp, but not CTLP, lysed erythrocytes. Msp complex (partially purified outer membranes free of protease activity) was cytotoxic toward a variety of different cell types. Pore-forming activities of recombinant Msp in black lipid model membrane assays and in HeLa cell membranes were similar to those reported for the native protein, supporting the hypothesis that Msp cytotoxicity was due to its pore-forming activity.
Persistent Identifierhttp://hdl.handle.net/10722/48927
ISSN
2015 Impact Factor: 3.603
2015 SCImago Journal Rankings: 2.342
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorFenno, JCen_HK
dc.contributor.authorHannam, PMen_HK
dc.contributor.authorLeung, WKen_HK
dc.contributor.authorTamura, Men_HK
dc.contributor.authorUitto, VJen_HK
dc.contributor.authorMcBride, BCen_HK
dc.date.accessioned2008-06-12T06:29:53Z-
dc.date.available2008-06-12T06:29:53Z-
dc.date.issued1998en_HK
dc.identifier.citationInfection And Immunity, 1998, v. 66 n. 5, p. 1869-1877en_HK
dc.identifier.issn0019-9567en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48927-
dc.description.abstractProminent antigens of Treponema denticola have been suggested to be mediators of the cytopathic effects typically seen in periodontal disease. In the present study of the T. denticola major surface protein (Msp) and the surface-expressed chymotrypsinlike protease complex (CTLP), we characterized the ability of these proteins to adhere to and lyse epithelial cells. Msp and CTLP were closely associated in spirochete outer membranes. Purified Msp, both native and recombinant, and CTLP bound to glutaraldehyde-fixed periodontal ligament epithelial cells. Adherence of Msp was partially blocked by specific antibodies. Adherence of CTLP was partially blocked by serine protease inhibitors and was further inhibited by specific antibodies. Both native Msp and CTLP were cytotoxic toward periodontal ligament epithelial cells, and their cytotoxicity was inhibited by the same treatments that inhibited adherence. Msp, but not CTLP, lysed erythrocytes. Msp complex (partially purified outer membranes free of protease activity) was cytotoxic toward a variety of different cell types. Pore-forming activities of recombinant Msp in black lipid model membrane assays and in HeLa cell membranes were similar to those reported for the native protein, supporting the hypothesis that Msp cytotoxicity was due to its pore-forming activity.en_HK
dc.format.extent418 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofInfection and Immunityen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsInfection and Immunity. Copyright © American Society for Microbiology.en_HK
dc.rightsCopyright © American Society for Microbiology, Infection and Immunity, 1998, v. 66 n. 5, p. 1869-1877en_HK
dc.subject.meshBacterial Outer Membrane Proteins - isolation & purification - toxicityen_HK
dc.subject.meshSerine Endopeptidases - toxicityen_HK
dc.subject.meshTreponema - pathogenicityen_HK
dc.subject.meshBacterial Adhesionen_HK
dc.subject.meshCHO Cellsen_HK
dc.titleCytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticolaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0019-9567&volume=66&issue=5&spage=1869&epage=1877&date=1998&atitle=Cytopathic+effects+of+the+major+surface+protein+and+the+chymotrypsinlike+protease+of+Treponema+denticolaen_HK
dc.identifier.emailLeung, WK:ewkleung@hkucc.hku.hken_HK
dc.identifier.authorityLeung, WK=rp00019en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid9573063-
dc.identifier.pmcidPMC108137-
dc.identifier.scopuseid_2-s2.0-0031900968en_HK
dc.identifier.hkuros32924-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031900968&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume66en_HK
dc.identifier.issue5en_HK
dc.identifier.spage1869en_HK
dc.identifier.epage1877en_HK
dc.identifier.isiWOS:000073413100009-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridFenno, JC=6602072985en_HK
dc.identifier.scopusauthoridHannam, PM=6602614873en_HK
dc.identifier.scopusauthoridLeung, WK=25224691800en_HK
dc.identifier.scopusauthoridTamura, M=8773768700en_HK
dc.identifier.scopusauthoridUitto, VJ=7004455896en_HK
dc.identifier.scopusauthoridMcBride, BC=7102465580en_HK

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