Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor
Identifieur interne : 001113 ( Pmc/Checkpoint ); précédent : 001112; suivant : 001114Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor
Auteurs : Dong P. Han [États-Unis] ; Adam Penn-Nicholson [États-Unis] ; Michael W. Cho [États-Unis]Source :
- Virology [ 0042-6822 ] ; 2006.
Abstract
Severe acute respiratory syndrome (SARS) is caused by a novel coronavirus, SARS-CoV. Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2). Alanine scanning mutagenesis analysis was performed to identify determinants on ACE2 critical for SARS-CoV infection. Results indicated that charged amino acids between residues 22 and 57 were important, K26 and D30, in particular. Peptides representing various regions of ACE2 critical for virus infection were chemically synthesized and evaluated for antiviral activity. Two peptides (a.a. 22–44 and 22–57) exhibited a modest antiviral activity with IC50 of about 50 μM and 6 μM, respectively. One peptide comprised of two discontinuous segments of ACE2 (a.a. 22–44 and 351–357) artificially linked together by glycine, exhibited a potent antiviral activity with IC50 of about 0.1 μM. This novel peptide is a promising candidate as a therapeutic agent against this deadly emerging pathogen.
Url:
DOI: 10.1016/j.virol.2006.01.029
PubMed: 16510163
PubMed Central: 7111894
Affiliations:
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Han</name><affiliation wicri:level="2"><nlm:aff id="aff1">Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Penn Nicholson, Adam" sort="Penn Nicholson, Adam" uniqKey="Penn Nicholson A" first="Adam" last="Penn-Nicholson">Adam Penn-Nicholson</name><affiliation wicri:level="2"><nlm:aff id="aff1">Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. 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Han</name><affiliation wicri:level="2"><nlm:aff id="aff1">Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Penn Nicholson, Adam" sort="Penn Nicholson, Adam" uniqKey="Penn Nicholson A" first="Adam" last="Penn-Nicholson">Adam Penn-Nicholson</name><affiliation wicri:level="2"><nlm:aff id="aff1">Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author><author><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><affiliation wicri:level="2"><nlm:aff id="aff1">Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="aff2">Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation><affiliation wicri:level="2"><nlm:aff id="aff3">Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, OH 44106</wicri:regionArea><placeName><region type="state">Ohio</region></placeName></affiliation></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Severe acute respiratory syndrome (SARS) is caused by a novel coronavirus, SARS-CoV. Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2). Alanine scanning mutagenesis analysis was performed to identify determinants on ACE2 critical for SARS-CoV infection. Results indicated that charged amino acids between residues 22 and 57 were important, K26 and D30, in particular. Peptides representing various regions of ACE2 critical for virus infection were chemically synthesized and evaluated for antiviral activity. Two peptides (a.a. 22–44 and 22–57) exhibited a modest antiviral activity with IC<sub>50</sub> of about 50 μM and 6 μM, respectively. One peptide comprised of two discontinuous segments of ACE2 (a.a. 22–44 and 351–357) artificially linked together by glycine, exhibited a potent antiviral activity with IC<sub>50</sub> of about 0.1 μM. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Virology</journal-id><journal-id journal-id-type="iso-abbrev">Virology</journal-id><journal-title-group><journal-title>Virology</journal-title></journal-title-group><issn pub-type="ppub">0042-6822</issn><issn pub-type="epub">1096-0341</issn><publisher><publisher-name>Elsevier Inc.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">16510163</article-id><article-id pub-id-type="pmc">7111894</article-id><article-id pub-id-type="publisher-id">S0042-6822(06)00033-X</article-id><article-id pub-id-type="doi">10.1016/j.virol.2006.01.029</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Identification of critical determinants on ACE2 for SARS-CoV entry and development of a potent entry inhibitor</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Han</surname><given-names>Dong P.</given-names></name><xref rid="aff1" ref-type="aff">a</xref></contrib><contrib contrib-type="author"><name><surname>Penn-Nicholson</surname><given-names>Adam</given-names></name><xref rid="aff1" ref-type="aff">a</xref></contrib><contrib contrib-type="author"><name><surname>Cho</surname><given-names>Michael W.</given-names></name><email>mcho@case.edu</email><xref rid="aff1" ref-type="aff">a</xref><xref rid="aff2" ref-type="aff">b</xref><xref rid="aff3" ref-type="aff">c</xref><xref rid="cor1" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="aff1"><label>a</label>Department of Medicine, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</aff><aff id="aff2"><label>b</label>Department of Biochemistry, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</aff><aff id="aff3"><label>c</label>Department of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA</aff><author-notes><corresp id="cor1"><label>⁎</label>Corresponding author. Department of Medicine, Division of Infectious Diseases, Case Western Reserve University School of Medicine, 10900 Euclid Avenue, Cleveland, OH 44106-4984, USA. Fax: +1 216 368 0069. <email>mcho@case.edu</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>28</day><month>2</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"><day>20</day><month>6</month><year>2006</year></pub-date><pub-date pub-type="epub"><day>28</day><month>2</month><year>2006</year></pub-date><volume>350</volume><issue>1</issue><fpage>15</fpage><lpage>25</lpage><history><date date-type="received"><day>23</day><month>11</month><year>2005</year></date><date date-type="accepted"><day>14</day><month>1</month><year>2006</year></date></history><permissions><copyright-statement>Copyright © 2006 Elsevier Inc. All rights reserved.</copyright-statement><copyright-year>2006</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>Severe acute respiratory syndrome (SARS) is caused by a novel coronavirus, SARS-CoV. Virus entry into cells is mediated through interactions between spike (S) glycoprotein and angiotensin-converting enzyme 2 (ACE2). Alanine scanning mutagenesis analysis was performed to identify determinants on ACE2 critical for SARS-CoV infection. Results indicated that charged amino acids between residues 22 and 57 were important, K26 and D30, in particular. Peptides representing various regions of ACE2 critical for virus infection were chemically synthesized and evaluated for antiviral activity. Two peptides (a.a. 22–44 and 22–57) exhibited a modest antiviral activity with IC<sub>50</sub> of about 50 μM and 6 μM, respectively. One peptide comprised of two discontinuous segments of ACE2 (a.a. 22–44 and 351–357) artificially linked together by glycine, exhibited a potent antiviral activity with IC<sub>50</sub> of about 0.1 μM. This novel peptide is a promising candidate as a therapeutic agent against this deadly emerging pathogen.</p></abstract><kwd-group><title>Keywords</title><kwd>SARS-CoV</kwd><kwd>Pseudovirus</kwd><kwd>ACE2</kwd><kwd>Peptide</kwd><kwd>Entry inhibitor</kwd></kwd-group></article-meta></front></pmc><affiliations><list><country><li>États-Unis</li></country><region><li>Ohio</li></region></list><tree><country name="États-Unis"><region name="Ohio"><name sortKey="Han, Dong P" sort="Han, Dong P" uniqKey="Han D" first="Dong P." last="Han">Dong P. Han</name></region><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><name sortKey="Cho, Michael W" sort="Cho, Michael W" uniqKey="Cho M" first="Michael W." last="Cho">Michael W. Cho</name><name sortKey="Penn Nicholson, Adam" sort="Penn Nicholson, Adam" uniqKey="Penn Nicholson A" first="Adam" last="Penn-Nicholson">Adam Penn-Nicholson</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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