Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability
Identifieur interne : 001664 ( Pmc/Checkpoint ); précédent : 001663; suivant : 001665Expression of SARS-coronavirus envelope protein in Escherichia coli cells alters membrane permeability
Auteurs : Y. Liao [Singapour] ; J. Lescar [Singapour] ; J. P. Tam [Singapour] ; D. X. Liu [Singapour]Source :
- Biochemical and Biophysical Research Communications [ 0006-291X ] ; 2004.
Abstract
To promote viral entry, replication, release, and spread to neighboring cells, many cytolytic animal viruses encode proteins responsible for modification of host cell membrane permeability and for formation of ion channels in host cell membranes during their life cycles. In this study, we show that the envelope (E) protein of severe acute respiratory syndrome-associated coronavirus can induce membrane permeability changes when expressed in
Url:
DOI: 10.1016/j.bbrc.2004.10.050
PubMed: 15522242
PubMed Central: 7092894
Affiliations:
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<front><div type="abstract" xml:lang="en"><p>To promote viral entry, replication, release, and spread to neighboring cells, many cytolytic animal viruses encode proteins responsible for modification of host cell membrane permeability and for formation of ion channels in host cell membranes during their life cycles. In this study, we show that the envelope (E) protein of severe acute respiratory syndrome-associated coronavirus can induce membrane permeability changes when expressed in <italic>Escherichia coli</italic>
. E protein expressed in bacterial and mammalian cells under reducing conditions existed as monomers, but formed homodimer and homotrimer under non-reducing conditions. Site-directed mutagenesis studies revealed that two cysteine residues of the E protein were essential for oligomerization, leading to induction of membrane permeability. This is the first report demonstrating that a coronavirus-encoded protein could modify membrane permeability in <italic>E. coli</italic>
cells.</p>
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<front><journal-meta><journal-id journal-id-type="nlm-ta">Biochem Biophys Res Commun</journal-id>
<journal-id journal-id-type="iso-abbrev">Biochem. Biophys. Res. Commun</journal-id>
<journal-title-group><journal-title>Biochemical and Biophysical Research Communications</journal-title>
</journal-title-group>
<issn pub-type="ppub">0006-291X</issn>
<issn pub-type="epub">1090-2104</issn>
<publisher><publisher-name>Elsevier Inc.</publisher-name>
</publisher>
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<article-meta><article-id pub-id-type="pmid">15522242</article-id>
<article-id pub-id-type="pmc">7092894</article-id>
<article-id pub-id-type="publisher-id">S0006-291X(04)02295-8</article-id>
<article-id pub-id-type="doi">10.1016/j.bbrc.2004.10.050</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Expression of SARS-coronavirus envelope protein in <italic>Escherichia coli</italic>
cells alters membrane permeability</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Liao</surname>
<given-names>Y.</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Lescar</surname>
<given-names>J.</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Tam</surname>
<given-names>J.P.</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Liu</surname>
<given-names>D.X.</given-names>
</name>
<email>dxliu@imcb.a-star.edu.sg</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="cor1" ref-type="corresp">*</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>a</label>
School of Biological Science, Nanyang Technological University, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore</aff>
<aff id="aff2"><label>b</label>
Institute of Molecular and Cell Biology, 61 Biopolis Drive, Proteos, Singapore 138673, Singapore</aff>
<author-notes><corresp id="cor1"><label>*</label>
Corresponding author. Fax: +65 67791117 <email>dxliu@imcb.a-star.edu.sg</email>
</corresp>
</author-notes>
<pub-date pub-type="pmc-release"><day>30</day>
<month>10</month>
<year>2004</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><day>3</day>
<month>12</month>
<year>2004</year>
</pub-date>
<pub-date pub-type="epub"><day>30</day>
<month>10</month>
<year>2004</year>
</pub-date>
<volume>325</volume>
<issue>1</issue>
<fpage>374</fpage>
<lpage>380</lpage>
<history><date date-type="received"><day>27</day>
<month>9</month>
<year>2004</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2004 Elsevier Inc. All rights reserved.</copyright-statement>
<copyright-year>2004</copyright-year>
<copyright-holder>Elsevier Inc.</copyright-holder>
<license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p>
</license>
</permissions>
<abstract><p>To promote viral entry, replication, release, and spread to neighboring cells, many cytolytic animal viruses encode proteins responsible for modification of host cell membrane permeability and for formation of ion channels in host cell membranes during their life cycles. In this study, we show that the envelope (E) protein of severe acute respiratory syndrome-associated coronavirus can induce membrane permeability changes when expressed in <italic>Escherichia coli</italic>
. E protein expressed in bacterial and mammalian cells under reducing conditions existed as monomers, but formed homodimer and homotrimer under non-reducing conditions. Site-directed mutagenesis studies revealed that two cysteine residues of the E protein were essential for oligomerization, leading to induction of membrane permeability. This is the first report demonstrating that a coronavirus-encoded protein could modify membrane permeability in <italic>E. coli</italic>
cells.</p>
</abstract>
<kwd-group><title>Keywords</title>
<kwd>Severe acute respiratory syndrome coronavirus</kwd>
<kwd>Envelope protein</kwd>
<kwd>Membrane permeability</kwd>
<kwd><italic>Escherichia coli</italic>
</kwd>
<kwd>E protein</kwd>
<kwd>Oligomerization</kwd>
<kwd>Viroporin</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>Singapour</li>
</country>
</list>
<tree><country name="Singapour"><noRegion><name sortKey="Liao, Y" sort="Liao, Y" uniqKey="Liao Y" first="Y." last="Liao">Y. Liao</name>
</noRegion>
<name sortKey="Lescar, J" sort="Lescar, J" uniqKey="Lescar J" first="J." last="Lescar">J. Lescar</name>
<name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D. X." last="Liu">D. X. Liu</name>
<name sortKey="Liu, D X" sort="Liu, D X" uniqKey="Liu D" first="D. X." last="Liu">D. X. Liu</name>
<name sortKey="Tam, J P" sort="Tam, J P" uniqKey="Tam J" first="J. P." last="Tam">J. P. Tam</name>
</country>
</tree>
</affiliations>
</record>
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