The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers
In a direct test of the hypothesis that the M2 coat protein of influenza A can function as a proton translocator, we incorporated a synthetic peptide containing its putative transmembrane domain into voltage-clamped planar lipid bilayers. We observed single proton-selective ion channels with a condu...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 1992-09, Vol.190 (1), p.485-489 |
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| container_title | Virology (New York, N.Y.) |
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| creator | Duff, K.C. Ashley, R.H. |
| description | In a direct test of the hypothesis that the M2 coat protein of influenza A can function as a proton translocator, we incorporated a synthetic peptide containing its putative transmembrane domain into voltage-clamped planar lipid bilayers. We observed single proton-selective ion channels with a conductance of ∼10 pS at a pH of 2.3, consistent with the association of several monomers around a central water-filled pore. The channels were reversibly blocked by the anti-influenza drug amantadine. These experiments imply a central role for M2 protein in virus replication and assembly and may explain the mechanism of action of amantadine. Analogous proteins may have a similar function in other viruses, and these may be susceptible to similar antiviral agents. |
| doi_str_mv | 10.1016/0042-6822(92)91239-Q |
| format | Article |
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Psychology</subject><subject>influenza A virus</subject><subject>Influenza A virus - metabolism</subject><subject>Ion Channels - drug effects</subject><subject>Ion Channels - metabolism</subject><subject>Kinetics</subject><subject>Lipid Bilayers - metabolism</subject><subject>Microbiology</subject><subject>Morphology, structure, chemical composition, physicochemical properties</subject><subject>Protons</subject><subject>Viral Matrix Proteins - metabolism</subject><subject>Virology</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVtr3DAQhUVpSbZp_0EDeiihfXCj21rWSyCE3iAlBNJnMZZGRMGWt5J3If31lbtL8taCYDTMN4fDHELecfaJM96eM6ZE03ZCfDDio-FCmub2BVlxZtqGScVfktUTckxel_LAaq81OyJHXHZCKrkiu7t7pHOGVEYc-1qR-mmEmOgUaExh2GL6DfSS_hB0k6cZ6yRMeSwURkgz-JiwKZhKnOMO_yJTou4eUsKhVAW6GSBBpkPcRE_7OMAj5vKGvAowFHx7qCfk55fPd1ffmuubr9-vLq8bt5ZqbrAXDDrJg_HMh171kgu_rl8NgEZ00HLshFv3rVQYgHVchN5rv_ZCcqWNPCFne91q7NcWy2zHWBwO1RNO22K1FIyZjv8X5G2ntWQLqPagy1MpGYPd5DhCfrSc2SUXuxzdLke3pr4lF3tb104P-tt-RP-8tA-izt8f5lAcDKEm4WJ5wlT1qUVbsYs9Vo-Lu4jZFhcxOfQxo5utn-K_ffwBNrmq8w</recordid><startdate>19920901</startdate><enddate>19920901</enddate><creator>Duff, K.C.</creator><creator>Ashley, R.H.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope></search><sort><creationdate>19920901</creationdate><title>The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers</title><author>Duff, K.C. ; Ashley, R.H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-eb20a831f9d0dfb4b312d50df7aae928a61e82c5b634efa0812fbd7d5d2314793</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amantadine - pharmacology</topic><topic>Biological and medical sciences</topic><topic>Electric Conductivity</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>influenza A virus</topic><topic>Influenza A virus - metabolism</topic><topic>Ion Channels - drug effects</topic><topic>Ion Channels - metabolism</topic><topic>Kinetics</topic><topic>Lipid Bilayers - metabolism</topic><topic>Microbiology</topic><topic>Morphology, structure, chemical composition, physicochemical properties</topic><topic>Protons</topic><topic>Viral Matrix Proteins - metabolism</topic><topic>Virology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Duff, K.C.</creatorcontrib><creatorcontrib>Ashley, R.H.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Duff, K.C.</au><au>Ashley, R.H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>1992-09-01</date><risdate>1992</risdate><volume>190</volume><issue>1</issue><spage>485</spage><epage>489</epage><pages>485-489</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><coden>VIRLAX</coden><abstract>In a direct test of the hypothesis that the M2 coat protein of influenza A can function as a proton translocator, we incorporated a synthetic peptide containing its putative transmembrane domain into voltage-clamped planar lipid bilayers. We observed single proton-selective ion channels with a conductance of ∼10 pS at a pH of 2.3, consistent with the association of several monomers around a central water-filled pore. The channels were reversibly blocked by the anti-influenza drug amantadine. These experiments imply a central role for M2 protein in virus replication and assembly and may explain the mechanism of action of amantadine. Analogous proteins may have a similar function in other viruses, and these may be susceptible to similar antiviral agents.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1382343</pmid><doi>10.1016/0042-6822(92)91239-Q</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 1992-09, Vol.190 (1), p.485-489 |
| issn | 0042-6822 1096-0341 |
| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals |
| subjects | Amantadine - pharmacology Biological and medical sciences Electric Conductivity Fundamental and applied biological sciences. Psychology influenza A virus Influenza A virus - metabolism Ion Channels - drug effects Ion Channels - metabolism Kinetics Lipid Bilayers - metabolism Microbiology Morphology, structure, chemical composition, physicochemical properties Protons Viral Matrix Proteins - metabolism Virology |
| title | The transmembrane domain of influenza A M2 protein forms amantadine-sensitive proton channels in planar lipid bilayers |
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