Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride
A 63 residue peptide, p7, encoded by hepatitis C virus was synthesised and tested for ion channel activity in lipid bilayer membranes. Ion channels formed by p7 had a variable conductance: some channels had conductances as low as 14 pS. The reversal potential of currents flowing through the channels...
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| Veröffentlicht in: | FEBS letters 2004-01, Vol.557 (1), p.99-103 |
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| creator | Premkumar, A Wilson, L Ewart, G.D Gage, P.W |
| description | A 63 residue peptide, p7, encoded by hepatitis C virus was synthesised and tested for ion channel activity in lipid bilayer membranes. Ion channels formed by p7 had a variable conductance: some channels had conductances as low as 14 pS. The reversal potential of currents flowing through the channels formed by p7 showed that they were permeable to potassium and sodium ions and less permeable to calcium ions. Addition of Ca
2+ to solutions made channels formed by p7 less potassium- or sodium-selective. Hexamethylene amiloride, a drug previously shown to block ion channels formed by Vpu encoded by HIV-1, blocked channels formed by p7. In view of the increasing number of peptides encoded by viruses that have been shown to form ion channels, it is suggested that ion channels may play an important role in the life cycle of many viruses and that drugs that block these channels may prove to be useful antiviral agents. |
| doi_str_mv | 10.1016/S0014-5793(03)01453-4 |
| format | Article |
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2+ to solutions made channels formed by p7 less potassium- or sodium-selective. Hexamethylene amiloride, a drug previously shown to block ion channels formed by Vpu encoded by HIV-1, blocked channels formed by p7. In view of the increasing number of peptides encoded by viruses that have been shown to form ion channels, it is suggested that ion channels may play an important role in the life cycle of many viruses and that drugs that block these channels may prove to be useful antiviral agents.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(03)01453-4</identifier><identifier>PMID: 14741348</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amiloride - analogs & derivatives ; Amiloride - pharmacology ; Amino Acid Sequence ; Cation-selective ion channels ; Hepatitis C virus ; Hexamethylene amiloride ; Human immunodeficiency virus 1 ; Ion Channels - biosynthesis ; Ion Channels - drug effects ; Lipid Bilayers ; Membrane Potentials - drug effects ; Molecular Sequence Data ; Peptide Fragments - chemistry ; Peptide Fragments - pharmacology ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Viral Proteins - chemistry ; Viral Proteins - pharmacology</subject><ispartof>FEBS letters, 2004-01, Vol.557 (1), p.99-103</ispartof><rights>2003</rights><rights>FEBS Letters 557 (2004) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5094-4a313058808d8fe2fe5f8fc41992fc88f0e8a24c1cb6a6e2862183a4dcc0452a3</citedby><cites>FETCH-LOGICAL-c5094-4a313058808d8fe2fe5f8fc41992fc88f0e8a24c1cb6a6e2862183a4dcc0452a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2803%2901453-4$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579303014534$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14741348$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Premkumar, A</creatorcontrib><creatorcontrib>Wilson, L</creatorcontrib><creatorcontrib>Ewart, G.D</creatorcontrib><creatorcontrib>Gage, P.W</creatorcontrib><title>Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>A 63 residue peptide, p7, encoded by hepatitis C virus was synthesised and tested for ion channel activity in lipid bilayer membranes. Ion channels formed by p7 had a variable conductance: some channels had conductances as low as 14 pS. The reversal potential of currents flowing through the channels formed by p7 showed that they were permeable to potassium and sodium ions and less permeable to calcium ions. Addition of Ca
2+ to solutions made channels formed by p7 less potassium- or sodium-selective. Hexamethylene amiloride, a drug previously shown to block ion channels formed by Vpu encoded by HIV-1, blocked channels formed by p7. In view of the increasing number of peptides encoded by viruses that have been shown to form ion channels, it is suggested that ion channels may play an important role in the life cycle of many viruses and that drugs that block these channels may prove to be useful antiviral agents.</description><subject>Amiloride - analogs & derivatives</subject><subject>Amiloride - pharmacology</subject><subject>Amino Acid Sequence</subject><subject>Cation-selective ion channels</subject><subject>Hepatitis C virus</subject><subject>Hexamethylene amiloride</subject><subject>Human immunodeficiency virus 1</subject><subject>Ion Channels - biosynthesis</subject><subject>Ion Channels - drug effects</subject><subject>Lipid Bilayers</subject><subject>Membrane Potentials - drug effects</subject><subject>Molecular Sequence Data</subject><subject>Peptide Fragments - chemistry</subject><subject>Peptide Fragments - pharmacology</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Viral Proteins - chemistry</subject><subject>Viral Proteins - pharmacology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhq0KRLeFn9DKJwSHgD8T51TBqqVIlTi0nC2vM9aaOvHWzm7Zf4-zWcGxSJbs8TzzzmhehC4o-UQJrT_fE0JFJZuWfyD8Y3lLXokTtKCq4RUXtXqFFn-RU3SW8y9SYkXbN-iUikZQLtQCuaUZfRyqDAHs6HeAS4Tt2gwDhIxdTD10eLXHmwZHh9ewKfzoM17inU_bjE0CvArRPs7YGn6bHsb1PsAA2PQ-xOQ7eIteOxMyvDve5-jnzfXD8ra6-_Ht-_LLXWUlaUUlDKecSKWI6pQD5kA65aygbcucVcoRUIYJS-2qNjUwVTOquBGdtURIZvg5ej_rblJ82kIede-zhRDMAHGbtSKUskbSF0HaENlIxgsoZ9CmmHMCpzfJ9ybtNSV6ckIfnNDTmjUpZ3JCi1J3eWywXZUV_qs6rr4AtzPw7APs_09V31x_ZYfMlCD88D31upqlimWw85B0th4GC51PxVXdRf_CtH8AotusCg</recordid><startdate>20040116</startdate><enddate>20040116</enddate><creator>Premkumar, A</creator><creator>Wilson, L</creator><creator>Ewart, G.D</creator><creator>Gage, P.W</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>20040116</creationdate><title>Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride</title><author>Premkumar, A ; Wilson, L ; Ewart, G.D ; Gage, P.W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5094-4a313058808d8fe2fe5f8fc41992fc88f0e8a24c1cb6a6e2862183a4dcc0452a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amiloride - analogs & derivatives</topic><topic>Amiloride - pharmacology</topic><topic>Amino Acid Sequence</topic><topic>Cation-selective ion channels</topic><topic>Hepatitis C virus</topic><topic>Hexamethylene amiloride</topic><topic>Human immunodeficiency virus 1</topic><topic>Ion Channels - biosynthesis</topic><topic>Ion Channels - drug effects</topic><topic>Lipid Bilayers</topic><topic>Membrane Potentials - drug effects</topic><topic>Molecular Sequence Data</topic><topic>Peptide Fragments - chemistry</topic><topic>Peptide Fragments - pharmacology</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Viral Proteins - chemistry</topic><topic>Viral Proteins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Premkumar, A</creatorcontrib><creatorcontrib>Wilson, L</creatorcontrib><creatorcontrib>Ewart, G.D</creatorcontrib><creatorcontrib>Gage, P.W</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Premkumar, A</au><au>Wilson, L</au><au>Ewart, G.D</au><au>Gage, P.W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-01-16</date><risdate>2004</risdate><volume>557</volume><issue>1</issue><spage>99</spage><epage>103</epage><pages>99-103</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>A 63 residue peptide, p7, encoded by hepatitis C virus was synthesised and tested for ion channel activity in lipid bilayer membranes. Ion channels formed by p7 had a variable conductance: some channels had conductances as low as 14 pS. The reversal potential of currents flowing through the channels formed by p7 showed that they were permeable to potassium and sodium ions and less permeable to calcium ions. Addition of Ca
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| subjects | Amiloride - analogs & derivatives Amiloride - pharmacology Amino Acid Sequence Cation-selective ion channels Hepatitis C virus Hexamethylene amiloride Human immunodeficiency virus 1 Ion Channels - biosynthesis Ion Channels - drug effects Lipid Bilayers Membrane Potentials - drug effects Molecular Sequence Data Peptide Fragments - chemistry Peptide Fragments - pharmacology Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Viral Proteins - chemistry Viral Proteins - pharmacology |
| title | Cation-selective ion channels formed by p7 of hepatitis C virus are blocked by hexamethylene amiloride |
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