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- Publisher Website: 10.1128/IAI.64.8.2904-2910.1996
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- PMID: 8757811
- WOS: WOS:A1996UY89300004
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Article: The major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes
Title | The major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes |
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Authors | |
Issue Date | 1996 |
Publisher | American Society for Microbiology. |
Citation | Infection And Immunity, 1996, v. 64 n. 8, p. 2904-2910 How to Cite? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/48925 |
ISSN | 2023 Impact Factor: 2.9 2023 SCImago Journal Rankings: 1.042 |
PubMed Central ID | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Mathers, DA | en_HK |
dc.contributor.author | Leung, WK | en_HK |
dc.contributor.author | Fenno, JC | en_HK |
dc.contributor.author | Hong, Y | en_HK |
dc.contributor.author | Mcbride, BC | en_HK |
dc.date.accessioned | 2008-06-12T06:29:50Z | - |
dc.date.available | 2008-06-12T06:29:50Z | - |
dc.date.issued | 1996 | en_HK |
dc.identifier.citation | Infection And Immunity, 1996, v. 64 n. 8, p. 2904-2910 | en_HK |
dc.identifier.issn | 0019-9567 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/48925 | - |
dc.description.abstract | The 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.extent | 386 bytes | - |
dc.format.mimetype | text/html | - |
dc.language | eng | en_HK |
dc.publisher | American Society for Microbiology. | en_HK |
dc.relation.ispartof | Infection and Immunity | en_HK |
dc.rights | Infection and Immunity. Copyright © American Society for Microbiology. | en_HK |
dc.rights | Copyright © American Society for Microbiology, Infection and Immunity, 1996, v. 64 n. 8, p. 2904-2910 | en_HK |
dc.subject.mesh | Bacterial Proteins | en_HK |
dc.subject.mesh | Cell Membrane - metabolism | en_HK |
dc.subject.mesh | Porins - chemistry - metabolism | en_HK |
dc.subject.mesh | Anions - metabolism | en_HK |
dc.subject.mesh | Cations - metabolism | en_HK |
dc.title | The major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://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+membranes | en_HK |
dc.identifier.email | Leung, WK:ewkleung@hkucc.hku.hk | en_HK |
dc.identifier.authority | Leung, WK=rp00019 | en_HK |
dc.description.nature | published_or_final_version | en_HK |
dc.identifier.doi | 10.1128/IAI.64.8.2904-2910.1996 | - |
dc.identifier.pmid | 8757811 | - |
dc.identifier.pmcid | PMC174165 | en_HK |
dc.identifier.scopus | eid_2-s2.0-0030017433 | en_HK |
dc.identifier.hkuros | 24963 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0030017433&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 64 | en_HK |
dc.identifier.issue | 8 | en_HK |
dc.identifier.spage | 2904 | en_HK |
dc.identifier.epage | 2910 | en_HK |
dc.identifier.isi | WOS:A1996UY89300004 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Mathers, DA=7005933980 | en_HK |
dc.identifier.scopusauthorid | Leung, WK=25224691800 | en_HK |
dc.identifier.scopusauthorid | Fenno, JC=6602072985 | en_HK |
dc.identifier.scopusauthorid | Hong, Y=37022371800 | en_HK |
dc.identifier.scopusauthorid | Mcbride, BC=7102465580 | en_HK |
dc.identifier.issnl | 0019-9567 | - |