Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism
Identifieur interne : 000929 ( Pmc/Checkpoint ); précédent : 000928; suivant : 000930Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism
Auteurs : T. Mehnert ; A. Routh ; P. J. Judge ; Y. H. Lam ; D. Fischer ; A. Watts ; W. B. FischerSource :
- Proteins [ 0887-3585 ] ; 2007.
Abstract
Vpu from HIV‐1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu1‐32) and mutant peptides (Vpu1‐32‐W23L, Vpu1‐32‐R31V, Vpu1‐32‐S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu1‐32‐W23L has a considerable flickering pattern in the recordings and longer open times than Vpu1‐32. Whilst recordings for Vpu1‐32‐R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu1‐32‐S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu1‐32‐W23L indicate Michaelis–Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics. Proteins 2008. © 2007 Wiley‐Liss, Inc.
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DOI: 10.1002/prot.21642
PubMed: 17910056
PubMed Central: 7167847
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Fischer</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation><affiliation><nlm:aff id="af2"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">17910056</idno><idno type="pmc">7167847</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7167847</idno><idno type="RBID">PMC:7167847</idno><idno type="doi">10.1002/prot.21642</idno><date when="2007">2007</date><idno type="wicri:Area/Pmc/Corpus">000797</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000797</idno><idno type="wicri:Area/Pmc/Curation">000797</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000797</idno><idno type="wicri:Area/Pmc/Checkpoint">000929</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000929</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism</title><author><name sortKey="Mehnert, T" sort="Mehnert, T" uniqKey="Mehnert T" first="T." last="Mehnert">T. Mehnert</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Routh, A" sort="Routh, A" uniqKey="Routh A" first="A." last="Routh">A. Routh</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Judge, P J" sort="Judge, P J" uniqKey="Judge P" first="P. J." last="Judge">P. J. Judge</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Lam, Y H" sort="Lam, Y H" uniqKey="Lam Y" first="Y. H." last="Lam">Y. H. Lam</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Fischer, D" sort="Fischer, D" uniqKey="Fischer D" first="D." last="Fischer">D. Fischer</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Watts, A" sort="Watts, A" uniqKey="Watts A" first="A." last="Watts">A. Watts</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation></author><author><name sortKey="Fischer, W B" sort="Fischer, W B" uniqKey="Fischer W" first="W. B." last="Fischer">W. B. Fischer</name><affiliation><nlm:aff id="af1"></nlm:aff></affiliation><affiliation><nlm:aff id="af2"></nlm:aff></affiliation></author></analytic><series><title level="j">Proteins</title><idno type="ISSN">0887-3585</idno><idno type="eISSN">1097-0134</idno><imprint><date when="2007">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Abstract</title><p>Vpu from HIV‐1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu<sub>1‐32</sub>) and mutant peptides (Vpu<sub>1‐32</sub>‐W23L, Vpu<sub>1‐32</sub>‐R31V, Vpu<sub>1‐32</sub>‐S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu<sub>1‐32</sub>‐W23L has a considerable flickering pattern in the recordings and longer open times than Vpu<sub>1‐32</sub>. Whilst recordings for Vpu<sub>1‐32</sub>‐R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu<sub>1‐32</sub>‐S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu<sub>1‐32</sub>‐W23L indicate Michaelis–Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics. Proteins 2008. © 2007 Wiley‐Liss, Inc.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Atassi, Mz" uniqKey="Atassi M">MZ Atassi</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proteins</journal-id><journal-id journal-id-type="iso-abbrev">Proteins</journal-id><journal-id journal-id-type="doi">10.1002/(ISSN)1097-0134</journal-id><journal-id journal-id-type="publisher-id">PROT</journal-id><journal-title-group><journal-title>Proteins</journal-title></journal-title-group><issn pub-type="ppub">0887-3585</issn><issn pub-type="epub">1097-0134</issn><publisher><publisher-name>Wiley Subscription Services, Inc., A Wiley Company</publisher-name><publisher-loc>Hoboken</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">17910056</article-id><article-id pub-id-type="pmc">7167847</article-id><article-id pub-id-type="doi">10.1002/prot.21642</article-id><article-id pub-id-type="publisher-id">PROT21642</article-id><article-categories><subj-group subj-group-type="overline"><subject>Research Article</subject></subj-group><subj-group subj-group-type="heading"><subject>Research Articles</subject></subj-group></article-categories><title-group><article-title>Biophysical characterization of Vpu from HIV‐1 suggests a channel‐pore dualism</article-title><alt-title alt-title-type="right-running-head">Biophysical Characterization of Vpu From HIV‐1</alt-title></title-group><contrib-group><contrib id="au1" contrib-type="author"><name><surname>Mehnert</surname><given-names>T.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref></contrib><contrib id="au2" contrib-type="author"><name><surname>Routh</surname><given-names>A.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref></contrib><contrib id="au3" contrib-type="author"><name><surname>Judge</surname><given-names>P. J.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref></contrib><contrib id="au4" contrib-type="author"><name><surname>Lam</surname><given-names>Y. H.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref></contrib><contrib id="au5" contrib-type="author"><name><surname>Fischer</surname><given-names>D.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref></contrib><contrib id="au6" contrib-type="author"><name><surname>Watts</surname><given-names>A.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref></contrib><contrib id="au7" contrib-type="author" corresp="yes"><name><surname>Fischer</surname><given-names>W. B.</given-names></name><xref ref-type="aff" rid="af1"><sup>1</sup></xref><xref ref-type="aff" rid="af2"><sup>2</sup></xref><address><email>wfischer@ym.edu.tw</email></address></contrib></contrib-group><aff id="af1"><label><sup>1</sup></label>Biomembrane Structure Unit, Department of Biochemistry, Oxford University, Oxford OX1 3QU, United Kingdom</aff><aff id="af2"><label><sup>2</sup></label>Bionanotechnology Interdisciplinary Research Collaboration, Clarendon Laboratory, Department of Physics, Oxford University, Oxford OX1 3PU, United Kingdom</aff><author-notes><corresp id="correspondenceTo"><label>*</label>Institute of Biophotonics, School of Biomedical Science and Engineering, National Yang‐Ming University, 155, Sec. 2, Li‐Nong St., Taipei 112, Taiwan Republic of China===</corresp></author-notes><pub-date pub-type="epub"><day>01</day><month>10</month><year>2007</year></pub-date><pub-date pub-type="ppub"><month>3</month><year>2008</year></pub-date><volume>70</volume><issue>4</issue><issue-id pub-id-type="doi">10.1002/prot.v70:4</issue-id><fpage>1488</fpage><lpage>1497</lpage><history><date date-type="received"><day>19</day><month>2</month><year>2007</year></date><date date-type="rev-recd"><day>22</day><month>4</month><year>2007</year></date><date date-type="accepted"><day>17</day><month>5</month><year>2007</year></date></history><permissions><copyright-statement content-type="article-copyright">Copyright © 2007 Wiley‐Liss, Inc.</copyright-statement><license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="file:PROT-70-1488.pdf"></self-uri><abstract><title>Abstract</title><p>Vpu from HIV‐1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu<sub>1‐32</sub>) and mutant peptides (Vpu<sub>1‐32</sub>‐W23L, Vpu<sub>1‐32</sub>‐R31V, Vpu<sub>1‐32</sub>‐S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a main conductance level of around 20 pS. Vpu<sub>1‐32</sub>‐W23L has a considerable flickering pattern in the recordings and longer open times than Vpu<sub>1‐32</sub>. Whilst recordings for Vpu<sub>1‐32</sub>‐R31V are almost indistinguishable from those of the WT peptide, recordings for Vpu<sub>1‐32</sub>‐S24L do not exhibit any noticeable channel activity. Recordings of WT peptide and Vpu<sub>1‐32</sub>‐W23L indicate Michaelis–Menten behavior when the salt concentration is increased. Both peptide channels follow the Eisenman series I, indicative for a weak ion channel with almost pore like characteristics. Proteins 2008. © 2007 Wiley‐Liss, Inc.</p></abstract><kwd-group kwd-group-type="author-generated"><kwd id="kwd1">Vpu</kwd><kwd id="kwd2">HIV‐1</kwd><kwd id="kwd3">membrane proteins</kwd><kwd id="kwd4">artificial bilayers</kwd><kwd id="kwd5">ion channels</kwd><kwd id="kwd6">gating</kwd></kwd-group><funding-group><award-group id="funding-0001"><funding-source>Bionanotechnology IRC</funding-source></award-group><award-group id="funding-0002"><funding-source>MRC</funding-source></award-group></funding-group><counts><fig-count count="5"></fig-count><table-count count="1"></table-count><ref-count count="52"></ref-count><page-count count="10"></page-count><word-count count="6436"></word-count></counts><custom-meta-group><custom-meta><meta-name>source-schema-version-number</meta-name><meta-value>2.0</meta-value></custom-meta><custom-meta><meta-name>cover-date</meta-name><meta-value>March 2008</meta-value></custom-meta><custom-meta><meta-name>details-of-publishers-convertor</meta-name><meta-value>Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Fischer, D" sort="Fischer, D" uniqKey="Fischer D" first="D." last="Fischer">D. Fischer</name><name sortKey="Fischer, W B" sort="Fischer, W B" uniqKey="Fischer W" first="W. B." last="Fischer">W. B. Fischer</name><name sortKey="Judge, P J" sort="Judge, P J" uniqKey="Judge P" first="P. J." last="Judge">P. J. Judge</name><name sortKey="Lam, Y H" sort="Lam, Y H" uniqKey="Lam Y" first="Y. H." last="Lam">Y. H. Lam</name><name sortKey="Mehnert, T" sort="Mehnert, T" uniqKey="Mehnert T" first="T." last="Mehnert">T. Mehnert</name><name sortKey="Routh, A" sort="Routh, A" uniqKey="Routh A" first="A." last="Routh">A. Routh</name><name sortKey="Watts, A" sort="Watts, A" uniqKey="Watts A" first="A." last="Watts">A. Watts</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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