Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
Identifieur interne : 001104 ( Pmc/Checkpoint ); précédent : 001103; suivant : 001105Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein
Auteurs : Bruno Sainz [États-Unis] ; Eric C. Mossel [États-Unis] ; William R. Gallaher [États-Unis] ; William C. Wimley [États-Unis] ; C. J. Peters [États-Unis] ; Russell B. Wilson [États-Unis] ; Robert F. Garry [États-Unis]Source :
- Virus Research [ 0168-1702 ] ; 2006.
Abstract
Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002–2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40–70% at concentrations of 15–30 μM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2–4 μM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.
Url:
DOI: 10.1016/j.virusres.2006.03.001
PubMed: 16616792
PubMed Central: 2582734
Affiliations:
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<front><div type="abstract" xml:lang="en"><p>Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002–2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40–70% at concentrations of 15–30 μM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2–4 μM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.</p>
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</back>
</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Virus Res</journal-id>
<journal-id journal-id-type="iso-abbrev">Virus Res</journal-id>
<journal-title-group><journal-title>Virus Research</journal-title>
</journal-title-group>
<issn pub-type="ppub">0168-1702</issn>
<issn pub-type="epub">1872-7492</issn>
<publisher><publisher-name>Elsevier B.V.</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">16616792</article-id>
<article-id pub-id-type="pmc">2582734</article-id>
<article-id pub-id-type="publisher-id">S0168-1702(06)00074-8</article-id>
<article-id pub-id-type="doi">10.1016/j.virusres.2006.03.001</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Article</subject>
</subj-group>
</article-categories>
<title-group><article-title>Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Sainz</surname>
<given-names>Bruno</given-names>
<suffix>Jr.</suffix>
</name>
<email>bsainz@scripps.edu</email>
<xref rid="aff1" ref-type="aff">a</xref>
<xref rid="cor1" ref-type="corresp">⁎</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Mossel</surname>
<given-names>Eric C.</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="fn1" ref-type="fn">1</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Gallaher</surname>
<given-names>William R.</given-names>
</name>
<xref rid="aff3" ref-type="aff">c</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wimley</surname>
<given-names>William C.</given-names>
</name>
<xref rid="aff4" ref-type="aff">d</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Peters</surname>
<given-names>C.J.</given-names>
</name>
<xref rid="aff2" ref-type="aff">b</xref>
<xref rid="aff5" ref-type="aff">e</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Wilson</surname>
<given-names>Russell B.</given-names>
</name>
<xref rid="aff6" ref-type="aff">f</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Garry</surname>
<given-names>Robert F.</given-names>
</name>
<xref rid="aff1" ref-type="aff">a</xref>
</contrib>
</contrib-group>
<aff id="aff1"><label>a</label>
Department of Microbiology and Immunology, Tulane University Health Sciences Center, New Orleans, LA 70112, USA</aff>
<aff id="aff2"><label>b</label>
Department of Microbiology and Immunology,, University of Texas Medical Branch, Galveston, TX 77555, USA</aff>
<aff id="aff3"><label>c</label>
Department of Microbiology, Immunology and Parasitology, Louisiana State University Health Sciences Center, New Orleans, LA 70112, USA</aff>
<aff id="aff4"><label>d</label>
Department of Biochemistry, Tulane University Health Sciences Center, New Orleans, LA 70112, USA</aff>
<aff id="aff5"><label>e</label>
Department of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA</aff>
<aff id="aff6"><label>f</label>
Autoimmune Technologies, LLC, New Orleans, LA 70112, USA</aff>
<author-notes><corresp id="cor1"><label>⁎</label>
Corresponding author at: The Scripps Research Institute, Molecular and Experimental Medicine, 10550 N. Torrey Pines Rd, SBR-10, La Jolla, CA 92037, USA. Tel.: +1 858 784 2051; fax: +1 858 784 2960. <email>bsainz@scripps.edu</email>
</corresp>
<fn id="fn1"><label>1</label>
<p>Present address: Department of Microbiology, Immunology, and Pathology, Colorado State University, Fort Collins, CO 80523-1619, USA.</p>
</fn>
</author-notes>
<pub-date pub-type="pmc-release"><day>17</day>
<month>4</month>
<year>2006</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"><month>9</month>
<year>2006</year>
</pub-date>
<pub-date pub-type="epub"><day>17</day>
<month>4</month>
<year>2006</year>
</pub-date>
<volume>120</volume>
<issue>1</issue>
<fpage>146</fpage>
<lpage>155</lpage>
<history><date date-type="received"><day>20</day>
<month>7</month>
<year>2005</year>
</date>
<date date-type="rev-recd"><day>9</day>
<month>2</month>
<year>2006</year>
</date>
<date date-type="accepted"><day>1</day>
<month>3</month>
<year>2006</year>
</date>
</history>
<permissions><copyright-statement>Copyright © 2006 Elsevier B.V. All rights reserved.</copyright-statement>
<copyright-year>2006</copyright-year>
<copyright-holder>Elsevier B.V.</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>Severe acute respiratory syndrome-associated coronavirus (SARS-CoV) is the cause of an atypical pneumonia that affected Asia, North America and Europe in 2002–2003. The viral spike (S) glycoprotein is responsible for mediating receptor binding and membrane fusion. Recent studies have proposed that the carboxyl terminal portion (S2 subunit) of the S protein is a class I viral fusion protein. The Wimley and White interfacial hydrophobicity scale was used to identify regions within the CoV S2 subunit that may preferentially associate with lipid membranes with the premise that peptides analogous to these regions may function as inhibitors of viral infectivity. Five regions of high interfacial hydrophobicity spanning the length of the S2 subunit of SARS-CoV and murine hepatitis virus (MHV) were identified. Peptides analogous to regions of the N-terminus or the pre-transmembrane domain of the S2 subunit inhibited SARS-CoV plaque formation by 40–70% at concentrations of 15–30 μM. Interestingly, peptides analogous to the SARS-CoV or MHV loop region inhibited viral plaque formation by >80% at similar concentrations. The observed effects were dose-dependent (IC50 values of 2–4 μM) and not a result of peptide-mediated cell cytotoxicity. The antiviral activity of the CoV peptides tested provides an attractive basis for the development of new fusion peptide inhibitors corresponding to regions outside the fusion protein heptad repeat regions.</p>
</abstract>
<kwd-group><title>Keywords</title>
<kwd>Severe acute respiratory syndrome-associated coronavirus</kwd>
<kwd>Class I viral fusion protein</kwd>
<kwd>Peptide inhibitor</kwd>
<kwd>Murine hepatitis virus</kwd>
<kwd>Six-helix bundle</kwd>
<kwd>Anti-viral</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
<affiliations><list><country><li>États-Unis</li>
</country>
<region><li>Louisiane</li>
<li>Texas</li>
</region>
</list>
<tree><country name="États-Unis"><region name="Louisiane"><name sortKey="Sainz, Bruno" sort="Sainz, Bruno" uniqKey="Sainz B" first="Bruno" last="Sainz">Bruno Sainz</name>
</region>
<name sortKey="Gallaher, William R" sort="Gallaher, William R" uniqKey="Gallaher W" first="William R." last="Gallaher">William R. Gallaher</name>
<name sortKey="Garry, Robert F" sort="Garry, Robert F" uniqKey="Garry R" first="Robert F." last="Garry">Robert F. Garry</name>
<name sortKey="Mossel, Eric C" sort="Mossel, Eric C" uniqKey="Mossel E" first="Eric C." last="Mossel">Eric C. Mossel</name>
<name sortKey="Peters, C J" sort="Peters, C J" uniqKey="Peters C" first="C. J." last="Peters">C. J. Peters</name>
<name sortKey="Peters, C J" sort="Peters, C J" uniqKey="Peters C" first="C. J." last="Peters">C. J. Peters</name>
<name sortKey="Wilson, Russell B" sort="Wilson, Russell B" uniqKey="Wilson R" first="Russell B." last="Wilson">Russell B. Wilson</name>
<name sortKey="Wimley, William C" sort="Wimley, William C" uniqKey="Wimley W" first="William C." last="Wimley">William C. Wimley</name>
</country>
</tree>
</affiliations>
</record>
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