File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: The major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes

TitleThe major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes
Authors
Issue Date1996
PublisherAmerican Society for Microbiology.
Citation
Infection And Immunity, 1996, v. 64 n. 8, p. 2904-2910 How to Cite?
AbstractThe oral spirochete Treponema denticola is closely associated with periodontal diseases in humans. The 53-kDa major surface protein (Msp) located in the outer membrane of T. denticola serovar a (ATCC 35405) has both pure-forming activity and adhesin activity. We have used standard patch clamp recording methods to study the effects of a partially purified outer membrane complex containing Msp on HeLd cells. The Msp complex was free of the chymotrypsin-like proteinase also found in the outer membrane of T. denticola. Msp bound to several HeLd cell proteins, including a 65-kDa surface protein and a 96-kDa cytoplasmic protein. The Msp complex depolarized and increased the conductance of the HeLd cell membrane in a manner which was not strongly selective for Na+, K+, Ca2+, and Cl- ions. Cell-attached patches of HeLa cell membrane exposed to Msp complex exhibited short-lived channels with a slope conductance of 0.4 nS in physiologically normal saline. These studies show that Msp binds both a putative epithelial cell surface receptor and cytoplasmic proteins and that the Msp complex can form large conductance ion channels in the cytoplasmic membrane of epithelial cells. These properties may contribute to the cytopathic effects of T. denticola on host epithelial cells.
Persistent Identifierhttp://hdl.handle.net/10722/48925
ISSN
2015 Impact Factor: 3.603
2015 SCImago Journal Rankings: 2.342
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorMathers, DAen_HK
dc.contributor.authorLeung, WKen_HK
dc.contributor.authorFenno, JCen_HK
dc.contributor.authorHong, Yen_HK
dc.contributor.authorMcbride, BCen_HK
dc.date.accessioned2008-06-12T06:29:50Z-
dc.date.available2008-06-12T06:29:50Z-
dc.date.issued1996en_HK
dc.identifier.citationInfection And Immunity, 1996, v. 64 n. 8, p. 2904-2910en_HK
dc.identifier.issn0019-9567en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48925-
dc.description.abstractThe oral spirochete Treponema denticola is closely associated with periodontal diseases in humans. The 53-kDa major surface protein (Msp) located in the outer membrane of T. denticola serovar a (ATCC 35405) has both pure-forming activity and adhesin activity. We have used standard patch clamp recording methods to study the effects of a partially purified outer membrane complex containing Msp on HeLd cells. The Msp complex was free of the chymotrypsin-like proteinase also found in the outer membrane of T. denticola. Msp bound to several HeLd cell proteins, including a 65-kDa surface protein and a 96-kDa cytoplasmic protein. The Msp complex depolarized and increased the conductance of the HeLd cell membrane in a manner which was not strongly selective for Na+, K+, Ca2+, and Cl- ions. Cell-attached patches of HeLa cell membrane exposed to Msp complex exhibited short-lived channels with a slope conductance of 0.4 nS in physiologically normal saline. These studies show that Msp binds both a putative epithelial cell surface receptor and cytoplasmic proteins and that the Msp complex can form large conductance ion channels in the cytoplasmic membrane of epithelial cells. These properties may contribute to the cytopathic effects of T. denticola on host epithelial cells.en_HK
dc.format.extent386 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, 1996, v. 64 n. 8, p. 2904-2910en_HK
dc.subject.meshBacterial Proteinsen_HK
dc.subject.meshCell Membrane - metabolismen_HK
dc.subject.meshPorins - chemistry - metabolismen_HK
dc.subject.meshAnions - metabolismen_HK
dc.subject.meshCations - metabolismen_HK
dc.titleThe major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranesen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0019-9567&volume=64&issue=8&spage=2904&epage=2910&date=1996&atitle=The+major+surface+protein+complex+of+Treponema+denticola+depolarizes+and+induces+ion+channels+in+HeLa+cell+membranesen_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.pmid8757811-
dc.identifier.pmcidPMC174165en_HK
dc.identifier.scopuseid_2-s2.0-0030017433en_HK
dc.identifier.hkuros24963-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0030017433&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume64en_HK
dc.identifier.issue8en_HK
dc.identifier.spage2904en_HK
dc.identifier.epage2910en_HK
dc.identifier.isiWOS:A1996UY89300004-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridMathers, DA=7005933980en_HK
dc.identifier.scopusauthoridLeung, WK=25224691800en_HK
dc.identifier.scopusauthoridFenno, JC=6602072985en_HK
dc.identifier.scopusauthoridHong, Y=37022371800en_HK
dc.identifier.scopusauthoridMcbride, BC=7102465580en_HK

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats