Assembling an ion channel: ORF 3a from SARS-CoV.
Identifieur interne : 000657 ( PubMed/Corpus ); précédent : 000656; suivant : 000658Assembling 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 [ 1097-0282 ] ; 2013.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Lipid Bilayers.
- chemical : Ion Channels.
- Amino Acid Sequence, SARS Virus.
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.
DOI: 10.1002/bip.22230
PubMed: 23483519
Links to Exploration step
pubmed:23483519Le document en format XML
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<author><name sortKey="Chien, Tze Hsiang" sort="Chien, Tze Hsiang" uniqKey="Chien T" first="Tze-Hsiang" last="Chien">Tze-Hsiang Chien</name>
<affiliation><nlm:affiliation>Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang-Ming University, Taipei, 112, Taiwan.</nlm:affiliation>
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<author><name sortKey="Chiang, Ya Ling" sort="Chiang, Ya Ling" uniqKey="Chiang Y" first="Ya-Ling" last="Chiang">Ya-Ling Chiang</name>
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<author><name sortKey="Chen, Chin Pei" sort="Chen, Chin Pei" uniqKey="Chen C" first="Chin-Pei" last="Chen">Chin-Pei Chen</name>
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<author><name sortKey="Henklein, Petra" sort="Henklein, Petra" uniqKey="Henklein P" first="Petra" last="Henklein">Petra Henklein</name>
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<author><name sortKey="H Nel, Karen" sort="H Nel, Karen" uniqKey="H Nel K" first="Karen" last="H Nel">Karen H Nel</name>
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<author><name sortKey="Hwang, Ing Shouh" sort="Hwang, Ing Shouh" uniqKey="Hwang I" first="Ing-Shouh" last="Hwang">Ing-Shouh Hwang</name>
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<author><name sortKey="Willbold, Dieter" sort="Willbold, Dieter" uniqKey="Willbold D" first="Dieter" last="Willbold">Dieter Willbold</name>
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<author><name sortKey="Fischer, Wolfgang B" sort="Fischer, Wolfgang B" uniqKey="Fischer W" first="Wolfgang B" last="Fischer">Wolfgang B. Fischer</name>
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<series><title level="j">Biopolymers</title>
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
<CopyrightInformation>Copyright © 2013 Wiley Periodicals, Inc.</CopyrightInformation>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chien</LastName>
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