Detection of ion channel activity in Xenopus laevis oocytes expressing Influenza C virus CM2 protein
To demonstrate the ion channel activity of Influenza C virus CM2, we expressed this protein in oocytes of Xenopus laevis and measured whole cell currents by a two-electrode voltage-clamp method. It was found that the inward currents were induced upon hyperpolarizing the oocyte membranes. The amplitu...
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Veröffentlicht in: | Archives of virology 2004-01, Vol.149 (1), p.35-50 |
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description | To demonstrate the ion channel activity of Influenza C virus CM2, we expressed this protein in oocytes of Xenopus laevis and measured whole cell currents by a two-electrode voltage-clamp method. It was found that the inward currents were induced upon hyperpolarizing the oocyte membranes. The amplitude of the currents increased slowly with time during the hyperpolarizing pulse, and the current-voltage relationship was nonlinear, having a slope that increased with the level of hyperpolarization. These results suggest strongly that CM2 forms a voltage-activated ion channel. The current amplitude was increased to a small extent by lowering the external pH. We also found that the anti-influenza A virus drug amantadine hydrochloride failed to attenuate the inward currents of CM2-expressing oocytes induced by hyperpolarization. The reversal voltage of tail currents was affected by the reduction of [Cl-], but neither by the change of [Na+] nor by that of [K+]. Furthermore, the amplitude of the inward currents was decreased by an anion channel blocker. The data presented here suggest that CM2 protein forms a voltage-activated ion channel permeable to chloride ion. |
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It was found that the inward currents were induced upon hyperpolarizing the oocyte membranes. The amplitude of the currents increased slowly with time during the hyperpolarizing pulse, and the current-voltage relationship was nonlinear, having a slope that increased with the level of hyperpolarization. These results suggest strongly that CM2 forms a voltage-activated ion channel. The current amplitude was increased to a small extent by lowering the external pH. We also found that the anti-influenza A virus drug amantadine hydrochloride failed to attenuate the inward currents of CM2-expressing oocytes induced by hyperpolarization. The reversal voltage of tail currents was affected by the reduction of [Cl-], but neither by the change of [Na+] nor by that of [K+]. Furthermore, the amplitude of the inward currents was decreased by an anion channel blocker. The data presented here suggest that CM2 protein forms a voltage-activated ion channel permeable to chloride ion.</description><identifier>ISSN: 0304-8608</identifier><identifier>EISSN: 1432-8798</identifier><identifier>DOI: 10.1007/s00705-003-0209-3</identifier><identifier>PMID: 14689274</identifier><language>eng</language><publisher>Wien: Springer</publisher><subject>ACM2 protein ; amantadine hydrochloride ; Amino acids ; Animals ; Biological and medical sciences ; Chlorides - metabolism ; Fundamental and applied biological sciences. Psychology ; Glycoproteins ; Human viral diseases ; Infectious diseases ; Influenza ; Influenza C virus ; Ion Channels - metabolism ; Ion Transport ; Ions - metabolism ; Medical sciences ; Microbiology ; Miscellaneous ; Oocytes - physiology ; Patch-Clamp Techniques ; Plasmids ; Proteins ; Viral diseases ; Viral Matrix Proteins - metabolism ; Virology ; Xenopus laevis</subject><ispartof>Archives of virology, 2004-01, Vol.149 (1), p.35-50</ispartof><rights>2004 INIST-CNRS</rights><rights>Copyright Springer-Verlag 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-1ed68d3213f5da05b805ec8e8139ca6c7612ac664266a527fb334fd1c11d57fc3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15468164$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14689274$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>HONGO, S</creatorcontrib><creatorcontrib>ISHIL, K</creatorcontrib><creatorcontrib>MORI, K</creatorcontrib><creatorcontrib>TAKASHITA, E</creatorcontrib><creatorcontrib>MURAKI, Y</creatorcontrib><creatorcontrib>MATSUZAKI, Y</creatorcontrib><creatorcontrib>SUGAWARA, K</creatorcontrib><title>Detection of ion channel activity in Xenopus laevis oocytes expressing Influenza C virus CM2 protein</title><title>Archives of virology</title><addtitle>Arch Virol</addtitle><description>To demonstrate the ion channel activity of Influenza C virus CM2, we expressed this protein in oocytes of Xenopus laevis and measured whole cell currents by a two-electrode voltage-clamp method. It was found that the inward currents were induced upon hyperpolarizing the oocyte membranes. The amplitude of the currents increased slowly with time during the hyperpolarizing pulse, and the current-voltage relationship was nonlinear, having a slope that increased with the level of hyperpolarization. These results suggest strongly that CM2 forms a voltage-activated ion channel. The current amplitude was increased to a small extent by lowering the external pH. We also found that the anti-influenza A virus drug amantadine hydrochloride failed to attenuate the inward currents of CM2-expressing oocytes induced by hyperpolarization. The reversal voltage of tail currents was affected by the reduction of [Cl-], but neither by the change of [Na+] nor by that of [K+]. Furthermore, the amplitude of the inward currents was decreased by an anion channel blocker. The data presented here suggest that CM2 protein forms a voltage-activated ion channel permeable to chloride ion.</description><subject>ACM2 protein</subject><subject>amantadine hydrochloride</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Chlorides - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glycoproteins</subject><subject>Human viral diseases</subject><subject>Infectious diseases</subject><subject>Influenza</subject><subject>Influenza C virus</subject><subject>Ion Channels - metabolism</subject><subject>Ion Transport</subject><subject>Ions - metabolism</subject><subject>Medical sciences</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Oocytes - physiology</subject><subject>Patch-Clamp Techniques</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>Viral diseases</subject><subject>Viral Matrix Proteins - metabolism</subject><subject>Virology</subject><subject>Xenopus laevis</subject><issn>0304-8608</issn><issn>1432-8798</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqF0U2LFDEQBuAgiju7-gO8SBD01prKV6ePMqvrwooXBW8hk65olp5kTLoHx19vhhlY8OIlBeGpKpKXkBfA3gJj_bvaDqY6xkTHOBs68YisQAremX4wj8mKCSY7o5m5IJe13rMGmVBPyQVIbQbeyxUZr3FGP8ecaA70WPxPlxJO1LXbfZwPNCb6HVPeLZVODvex0pz9YcZK8feuYK0x_aC3KUwLpj-Oruk-lmbXnzndlTxjTM_Ik-Cmis_P9Yp8-_jh6_pTd_fl5nb9_q7zUsHcAY7ajIKDCGp0TG0MU-gNGhCDd9r3GrjzWkuutVO8DxshZBjBA4yqD15ckTenuW3vrwXrbLexepwmlzAv1RrGtIKe_xfCwLlWamjw1T_wPi8ltUdYDlyCUVI3BCfkS661YLC7EreuHCwwewzKnoKy7f_tMSgrWs_L8-Bls8XxoeOcTAOvz8BV76ZQXPKxPri22ICW4i_7cZqP</recordid><startdate>20040101</startdate><enddate>20040101</enddate><creator>HONGO, S</creator><creator>ISHIL, K</creator><creator>MORI, K</creator><creator>TAKASHITA, E</creator><creator>MURAKI, Y</creator><creator>MATSUZAKI, Y</creator><creator>SUGAWARA, K</creator><general>Springer</general><general>Springer Nature B.V</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>3V.</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20040101</creationdate><title>Detection of ion channel activity in Xenopus laevis oocytes expressing Influenza C virus CM2 protein</title><author>HONGO, S ; ISHIL, K ; MORI, K ; TAKASHITA, E ; MURAKI, Y ; MATSUZAKI, Y ; SUGAWARA, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-1ed68d3213f5da05b805ec8e8139ca6c7612ac664266a527fb334fd1c11d57fc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>ACM2 protein</topic><topic>amantadine hydrochloride</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Chlorides - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Glycoproteins</topic><topic>Human viral diseases</topic><topic>Infectious diseases</topic><topic>Influenza</topic><topic>Influenza C virus</topic><topic>Ion Channels - metabolism</topic><topic>Ion Transport</topic><topic>Ions - metabolism</topic><topic>Medical sciences</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Oocytes - physiology</topic><topic>Patch-Clamp Techniques</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>Viral diseases</topic><topic>Viral Matrix Proteins - metabolism</topic><topic>Virology</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>HONGO, S</creatorcontrib><creatorcontrib>ISHIL, K</creatorcontrib><creatorcontrib>MORI, K</creatorcontrib><creatorcontrib>TAKASHITA, E</creatorcontrib><creatorcontrib>MURAKI, Y</creatorcontrib><creatorcontrib>MATSUZAKI, Y</creatorcontrib><creatorcontrib>SUGAWARA, K</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>ProQuest Central (Corporate)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of virology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>HONGO, S</au><au>ISHIL, K</au><au>MORI, K</au><au>TAKASHITA, E</au><au>MURAKI, Y</au><au>MATSUZAKI, Y</au><au>SUGAWARA, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Detection of ion channel activity in Xenopus laevis oocytes expressing Influenza C virus CM2 protein</atitle><jtitle>Archives of virology</jtitle><addtitle>Arch Virol</addtitle><date>2004-01-01</date><risdate>2004</risdate><volume>149</volume><issue>1</issue><spage>35</spage><epage>50</epage><pages>35-50</pages><issn>0304-8608</issn><eissn>1432-8798</eissn><abstract>To demonstrate the ion channel activity of Influenza C virus CM2, we expressed this protein in oocytes of Xenopus laevis and measured whole cell currents by a two-electrode voltage-clamp method. It was found that the inward currents were induced upon hyperpolarizing the oocyte membranes. The amplitude of the currents increased slowly with time during the hyperpolarizing pulse, and the current-voltage relationship was nonlinear, having a slope that increased with the level of hyperpolarization. These results suggest strongly that CM2 forms a voltage-activated ion channel. The current amplitude was increased to a small extent by lowering the external pH. We also found that the anti-influenza A virus drug amantadine hydrochloride failed to attenuate the inward currents of CM2-expressing oocytes induced by hyperpolarization. The reversal voltage of tail currents was affected by the reduction of [Cl-], but neither by the change of [Na+] nor by that of [K+]. Furthermore, the amplitude of the inward currents was decreased by an anion channel blocker. The data presented here suggest that CM2 protein forms a voltage-activated ion channel permeable to chloride ion.</abstract><cop>Wien</cop><cop>New York, NY</cop><pub>Springer</pub><pmid>14689274</pmid><doi>10.1007/s00705-003-0209-3</doi><tpages>16</tpages></addata></record> |
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subjects | ACM2 protein amantadine hydrochloride Amino acids Animals Biological and medical sciences Chlorides - metabolism Fundamental and applied biological sciences. Psychology Glycoproteins Human viral diseases Infectious diseases Influenza Influenza C virus Ion Channels - metabolism Ion Transport Ions - metabolism Medical sciences Microbiology Miscellaneous Oocytes - physiology Patch-Clamp Techniques Plasmids Proteins Viral diseases Viral Matrix Proteins - metabolism Virology Xenopus laevis |
title | Detection of ion channel activity in Xenopus laevis oocytes expressing Influenza C virus CM2 protein |
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