Assembling an ion channel: ORF 3a from SARS‐CoV
Identifieur interne : 000327 ( Istex/Corpus ); précédent : 000326; suivant : 000328Assembling an ion channel: ORF 3a from SARS‐CoV
Auteurs : Tze-Hsiang Chien ; Ya-Ling Chiang ; Chin-Pei Chen ; Petra Henklein ; Karen H Nel ; Ing-Shouh Hwang ; Dieter Willbold ; Wolfgang B. FischerSource :
- Biopolymers [ 0006-3525 ] ; 2013-09.
English descriptors
- Teeft :
- A_id, Amino acids, Assembly process, Bilayer, Bilayer recordings, Biochim biophys acta, Biol, Biol chem, Biophys, Biopolymers, Buffer conditions, Cadmus, Calcium buffer, Channel, Channel activity, Channel protein, Channel recording data, Channel recordings, Chem, Conductance, Conductance levels, Conductance patterns, Conductance states, Contract grant sponsor, Customer a_id, Experimental data, Febs lett, Fischer, Full length, Full length protein, Fusion protein, Gating kinetics, Individual tmds, J_id, Linear regression analysis, Lipid, Lipid bilayer, Lipid bilayers, Lipid membrane, Lipid membranes, Manoharj, Manoharj time, Middle panel, Monomer, Negative voltages, Nicotinic acetylcholine, Peptide, Polytopic channel proteins, Pore, Positive voltage, Potassium buffer, Potassium channel, Potassium ions, Present study, Proc natl acad, Protein expression, Reconstituted, Room temperature, Selectivity, Stock solution, Tetrameric channel, Tmd1, Tmd2, Tmd3, Tmds, Viral channel, Wang, Weight ratio, Wiley periodicals.
Abstract
Protein 3a is a 274 amino acid polytopic channel protein with three putative transmembrane domains (TMDs) encoded by severe acute respiratory syndrome corona virus (SARS‐CoV). Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (PK ≈ 2 PCl) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. Biopolymers 99:628–635, 2013.
Url:
DOI: 10.1002/bip.22230
Links to Exploration step
ISTEX:AC2636A6D505B30CB630996CFA9C594A87F7561ALe document en format XML
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Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (PK ≈ 2 PCl) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. 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Fischer</name><affiliations><json:string>Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang‐Ming University, 112, Taipei, Taiwan</json:string><json:string>E-mail: wfischer@ym.edu.tw</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>ORF3a of SARS‐CoV</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>ion channel</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>self‐assembly</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>transmembrane peptides and proteins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>bilayer recordings</value></json:item></subject><articleId><json:string>BIP22230</json:string></articleId><arkIstex>ark:/67375/WNG-12XH5FZK-K</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>Protein 3a is a 274 amino acid polytopic channel protein with three putative transmembrane domains (TMDs) encoded by severe acute respiratory syndrome corona virus (SARS‐CoV). Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (PK ≈ 2 PCl) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. 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xml:id="author-0002"><persName><forename type="first">Chin‐Pei</forename><surname>Chen</surname></persName><affiliation><orgName type="division">Institute of Biophotonics, School of Biomedical Science and Engineering</orgName><orgName type="institution">National Yang‐Ming University</orgName><address><settlement>Taipei</settlement><street>112</street><country key="TW" xml:lang="en">TAIWAN, PROVINCE OF CHINA</country></address></affiliation></author><author xml:id="author-0003"><persName><forename type="first">Petra</forename><surname>Henklein</surname></persName><affiliation><orgName type="institution">Institute of Biochemistry, Charité‐Universitätsmedizin</orgName><address><street>Virchowweg 6, 10117</street><settlement>Berlin</settlement><country key="DE" xml:lang="en">GERMANY</country></address></affiliation></author><author xml:id="author-0004"><persName><forename type="first">Karen</forename><surname>Hänel</surname></persName><affiliation><orgName type="institution">Institute of 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Fischer; e‐mail: <email>wfischer@ym.edu.tw</email></correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:BIP.BIP22230.pdf"></link></linkGroup></publicationMeta><contentMeta><titleGroup><title type="main">Assembling an ion channel: ORF 3a from SARS‐CoV</title><title type="short">Assembling an Ion Channel: ORF 3a from SARS‐CoV</title><title type="shortAuthors">Chien et al</title></titleGroup><creators><creator affiliationRef="#bip22230-aff-0001" creatorRole="author" xml:id="bip22230-cr-0001"><personName><givenNames>Tze‐Hsiang</givenNames><familyName>Chien</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0002 #bip22230-aff-0003" creatorRole="author" xml:id="bip22230-cr-0002"><personName><givenNames>Ya‐Ling</givenNames><familyName>Chiang</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0001" creatorRole="author" xml:id="bip22230-cr-0003"><personName><givenNames>Chin‐Pei</givenNames><familyName>Chen</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0004" creatorRole="author" xml:id="bip22230-cr-0004"><personName><givenNames>Petra</givenNames><familyName>Henklein</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0005" creatorRole="author" xml:id="bip22230-cr-0005"><personName><givenNames>Karen</givenNames><familyName>Hänel</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0002 #bip22230-aff-0003" creatorRole="author" xml:id="bip22230-cr-0006"><personName><givenNames>Ing‐Shouh</givenNames><familyName>Hwang</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0005 #bip22230-aff-0006" creatorRole="author" xml:id="bip22230-cr-0007"><personName><givenNames>Dieter</givenNames><familyName>Willbold</familyName></personName></creator><creator affiliationRef="#bip22230-aff-0001" corresponding="yes" creatorRole="author" xml:id="bip22230-cr-0008"><personName><givenNames>Wolfgang B.</givenNames><familyName>Fischer</familyName></personName></creator></creators><affiliationGroup><affiliation countryCode="TW" type="organization" xml:id="bip22230-aff-0001"><orgDiv>Institute of Biophotonics, School of Biomedical Science and Engineering</orgDiv><orgName>National Yang‐Ming University</orgName><address><city>Taipei</city><street>112</street><country>Taiwan</country></address></affiliation><affiliation countryCode="TW" type="organization" xml:id="bip22230-aff-0002"><orgName>Institute of Physics</orgName><address><street>Academia Sinica, Nankang</street><city>Taipei</city><street>115</street><country>Taiwan</country></address></affiliation><affiliation countryCode="TW" type="organization" xml:id="bip22230-aff-0003"><orgDiv>Department of Material Science and Engineering</orgDiv><orgName>National Tsing Hua University</orgName><address><city>Hsinchu</city><postCode>300</postCode><country>Taiwan</country></address></affiliation><affiliation countryCode="DE" type="organization" xml:id="bip22230-aff-0004"><orgName>Institute of Biochemistry, Charité‐Universitätsmedizin</orgName><address><street>Virchowweg 6, 10117</street><city>Berlin</city><country>Germany</country></address></affiliation><affiliation countryCode="DE" type="organization" xml:id="bip22230-aff-0005"><orgName>Institute of Structural Biochemistry (ICS‐6), Research Center Jülich</orgName><address><city>Jülich</city><country>Germany</country></address></affiliation><affiliation countryCode="DE" type="organization" xml:id="bip22230-aff-0006"><orgName>Institut für Physikalische Biologie, Heinrich‐Heine‐Universität Düsseldorf</orgName><address><city>Düsseldorf</city><country>Germany</country></address></affiliation></affiliationGroup><keywordGroup type="author"><keyword xml:id="bip22230-kwd-0001">ORF3a of SARS‐CoV</keyword><keyword xml:id="bip22230-kwd-0002">ion channel</keyword><keyword xml:id="bip22230-kwd-0003">self‐assembly</keyword><keyword xml:id="bip22230-kwd-0004">transmembrane peptides and proteins</keyword><keyword xml:id="bip22230-kwd-0005">bilayer recordings</keyword></keywordGroup><fundingInfo><fundingAgency>National Science Council Taiwan
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</fundingAgency></fundingInfo><abstractGroup><abstract type="main"><title type="main">ABSTRACT</title><p>Protein 3a is a 274 amino acid polytopic channel protein with three putative transmembrane domains (TMDs) encoded by severe acute respiratory syndrome corona virus (SARS‐CoV). Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (<i>P</i><sub>K</sub> ≈ 2 P<sub>Cl</sub>) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. Biopolymers 99:628–635, 2013.</p></abstract></abstractGroup></contentMeta><noteGroup><note xml:id="bip22130-note-0001"><p>This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at <email>biopolymers@wiley.com</email></p></note></noteGroup></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Assembling an ion channel: ORF 3a from SARS‐CoV</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>Assembling an Ion Channel: ORF 3a from SARS‐CoV</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Assembling an ion channel: ORF 3a from SARS‐CoV</title></titleInfo><name type="personal"><namePart type="given">Tze‐Hsiang</namePart><namePart type="family">Chien</namePart><affiliation>Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang‐Ming University, 112, Taipei, Taiwan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ya‐Ling</namePart><namePart type="family">Chiang</namePart><affiliation>Institute of Physics, Academia Sinica, Nankang115, Taipei, Taiwan</affiliation><affiliation>Department of Material Science and Engineering, National Tsing Hua University, 300, Hsinchu, Taiwan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Chin‐Pei</namePart><namePart type="family">Chen</namePart><affiliation>Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang‐Ming University, 112, Taipei, Taiwan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Petra</namePart><namePart type="family">Henklein</namePart><affiliation>Institute of Biochemistry, Charité‐Universitätsmedizin, Virchowweg 6, 10117, Berlin, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Karen</namePart><namePart type="family">Hänel</namePart><affiliation>Institute of Structural Biochemistry (ICS‐6), Research Center Jülich, Jülich, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Ing‐Shouh</namePart><namePart type="family">Hwang</namePart><affiliation>Institute of Physics, Academia Sinica, Nankang115, Taipei, Taiwan</affiliation><affiliation>Department of Material Science and Engineering, National Tsing Hua University, 300, Hsinchu, Taiwan</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Dieter</namePart><namePart type="family">Willbold</namePart><affiliation>Institute of Structural Biochemistry (ICS‐6), Research Center Jülich, Jülich, Germany</affiliation><affiliation>Institut für Physikalische Biologie, Heinrich‐Heine‐Universität Düsseldorf, Düsseldorf, Germany</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Wolfgang B.</namePart><namePart type="family">Fischer</namePart><affiliation>Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang‐Ming University, 112, Taipei, Taiwan</affiliation><affiliation>E-mail: wfischer@ym.edu.tw</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-6N5SZHKN-D">article</genre><originInfo><publisher>Blackwell Publishing Ltd</publisher><dateIssued encoding="w3cdtf">2013-09</dateIssued><dateCreated encoding="w3cdtf">2013-03-22</dateCreated><dateCaptured encoding="w3cdtf">2012-09-08</dateCaptured><dateValid encoding="w3cdtf">2013-01-28</dateValid><copyrightDate encoding="w3cdtf">2013</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract>Protein 3a is a 274 amino acid polytopic channel protein with three putative transmembrane domains (TMDs) encoded by severe acute respiratory syndrome corona virus (SARS‐CoV). Synthetic peptides corresponding to each of its three individual transmembrane domains (TMDs) are reconstituted into artificial lipid bilayers. Only TMD2 and TMD3 induce channel activity. Reconstitution of the peptides as TMD1 + TMD3 as well as TMD2 + TMD3 in a 1 : 1 mixture induces membrane activity for both mixtures. In a 1 : 1 : 1 mixture, channel like behavior is almost restored. Expression of full length 3a and reconstitution into artificial lipid bilayers reveal a weak cation selective (PK ≈ 2 PCl) rectifying channel. In the presence of nonphysiological concentration of Ca‐ions the channel develops channel activity. © 2013 Wiley Periodicals, Inc. Biopolymers 99:628–635, 2013.</abstract><note type="funding">National Science Council Taiwan - No. NSC98‐2112‐M‐010‐002‐MY3; </note><note type="funding">German Academic Exchange Program (DAAD)</note><subject><genre>keywords</genre><topic>ORF3a of SARS‐CoV</topic><topic>ion channel</topic><topic>self‐assembly</topic><topic>transmembrane peptides and proteins</topic><topic>bilayer recordings</topic></subject><relatedItem type="host"><titleInfo><title>Biopolymers</title><subTitle>Original Research on Biomolecules</subTitle></titleInfo><titleInfo type="abbreviated"><title>Biopolymers</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><subject><genre>article-category</genre><topic>Research Article</topic><topic>Research Articles</topic></subject><identifier type="ISSN">0006-3525</identifier><identifier type="eISSN">1097-0282</identifier><identifier type="DOI">10.1002/(ISSN)1097-0282</identifier><identifier type="PublisherID">BIP</identifier><part><date>2013</date><detail type="volume"><caption>vol.</caption><number>99</number></detail><detail type="issue"><caption>no.</caption><number>9</number></detail><extent unit="pages"><start>628</start><end>635</end><total>8</total></extent></part></relatedItem><relatedItem type="references" displayLabel="bip22230-cit-0001"><titleInfo><title>Proc Natl Acad Sci USA</title></titleInfo><genre>journal-article</genre><note type="citation/reference">Walters, R. 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