Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells
Identifieur interne : 001579 ( Pmc/Curation ); précédent : 001578; suivant : 001580Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells
Auteurs : Jean Kaoru Millet ; Gary R. WhittakerSource :
- Virology [ 0042-6822 ] ; 2017.
Abstract
During viral entry, enveloped viruses require the fusion of their lipid envelope with host cell membranes. For coronaviruses, this critical step is governed by the virally-encoded spike (S) protein, a class I viral fusion protein that has several unique features. Coronavirus entry is unusual in that it is often biphasic in nature, and can occur at or near the cell surface or in late endosomes. Recent advances in structural, biochemical and molecular biology of the coronavirus S protein has shed light on the intricacies of coronavirus entry, in particular the molecular triggers of coronavirus S-mediated membrane fusion. Furthermore, characterization of the coronavirus fusion peptide (FP), the segment of the fusion protein that inserts to a target lipid bilayer during membrane fusion, has revealed its particular attributes which imparts some of the unusual properties of the S protein, such as Ca2+-dependency. These unusual characteristics can explain at least in part the biphasic nature of coronavirus entry. In this review, using severe acute respiratory syndrome coronavirus (SARS-CoV) as model virus, we give an overview of advances in research on the coronavirus fusion peptide with an emphasis on its role and properties within the biological context of host cell entry.
Url:
DOI: 10.1016/j.virol.2017.12.015
PubMed: 29275820
PubMed Central: 7112017
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells</title><author><name sortKey="Millet, Jean Kaoru" sort="Millet, Jean Kaoru" uniqKey="Millet J" first="Jean Kaoru" last="Millet">Jean Kaoru Millet</name></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">29275820</idno><idno type="pmc">7112017</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7112017</idno><idno type="RBID">PMC:7112017</idno><idno type="doi">10.1016/j.virol.2017.12.015</idno><date when="2017">2017</date><idno type="wicri:Area/Pmc/Corpus">001579</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001579</idno><idno type="wicri:Area/Pmc/Curation">001579</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001579</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells</title><author><name sortKey="Millet, Jean Kaoru" sort="Millet, Jean Kaoru" uniqKey="Millet J" first="Jean Kaoru" last="Millet">Jean Kaoru Millet</name></author><author><name sortKey="Whittaker, Gary R" sort="Whittaker, Gary R" uniqKey="Whittaker G" first="Gary R." last="Whittaker">Gary R. Whittaker</name></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2017">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>During viral entry, enveloped viruses require the fusion of their lipid envelope with host cell membranes. For coronaviruses, this critical step is governed by the virally-encoded spike (S) protein, a class I viral fusion protein that has several unique features. Coronavirus entry is unusual in that it is often biphasic in nature, and can occur at or near the cell surface or in late endosomes. Recent advances in structural, biochemical and molecular biology of the coronavirus S protein has shed light on the intricacies of coronavirus entry, in particular the molecular triggers of coronavirus S-mediated membrane fusion. Furthermore, characterization of the coronavirus fusion peptide (FP), the segment of the fusion protein that inserts to a target lipid bilayer during membrane fusion, has revealed its particular attributes which imparts some of the unusual properties of the S protein, such as Ca<sup>2+</sup>-dependency. These unusual characteristics can explain at least in part the biphasic nature of coronavirus entry. In this review, using severe acute respiratory syndrome coronavirus (SARS-CoV) as model virus, we give an overview of advances in research on the coronavirus fusion peptide with an emphasis on its role and properties within the biological context of host cell entry.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Apellaniz, B" uniqKey="Apellaniz B">B. Apellaniz</name></author><author><name sortKey="Huarte, N" uniqKey="Huarte N">N. Huarte</name></author><author><name sortKey="Largo, E" uniqKey="Largo E">E. 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Shi</name></author><author><name sortKey="Lian, G" uniqKey="Lian G">G. Lian</name></author><author><name sortKey="Wang, W" uniqKey="Wang W">W. Wang</name></author><author><name sortKey="Yin, X" uniqKey="Yin X">X. Yin</name></author><author><name sortKey="Zhao, Y" uniqKey="Zhao Y">Y. Zhao</name></author><author><name sortKey="Qu, X" uniqKey="Qu X">X. Qu</name></author><author><name sortKey="Ding, M" uniqKey="Ding M">M. Ding</name></author><author><name sortKey="Deng, H" uniqKey="Deng H">H. Deng</name></author></analytic></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">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">29275820</article-id><article-id pub-id-type="pmc">7112017</article-id><article-id pub-id-type="publisher-id">S0042-6822(17)30420-8</article-id><article-id pub-id-type="doi">10.1016/j.virol.2017.12.015</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells</article-title></title-group><contrib-group><contrib contrib-type="author" id="au0005"><name><surname>Millet</surname><given-names>Jean Kaoru</given-names></name></contrib><contrib contrib-type="author" id="au0010"><name><surname>Whittaker</surname><given-names>Gary R.</given-names></name><email>gary.whittaker@cornell.edu</email><xref rid="cor1" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="aff0005">Department of Microbiology and Immunology, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, United States</aff><author-notes><corresp id="cor1"><label>⁎</label>Correspondence to: Department of Microbiology & Immunology, C4-127 VMC, Cornell University, Ithaca, NY 14853, United States. <email>gary.whittaker@cornell.edu</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>21</day><month>12</month><year>2017</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>4</month><year>2018</year></pub-date><pub-date pub-type="epub"><day>21</day><month>12</month><year>2017</year></pub-date><volume>517</volume><fpage>3</fpage><lpage>8</lpage><history><date date-type="received"><day>31</day><month>10</month><year>2017</year></date><date date-type="rev-recd"><day>13</day><month>12</month><year>2017</year></date><date date-type="accepted"><day>15</day><month>12</month><year>2017</year></date></history><permissions><copyright-statement>© 2017 Elsevier Inc.</copyright-statement><copyright-year>2017</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 id="ab0010"><p>During viral entry, enveloped viruses require the fusion of their lipid envelope with host cell membranes. For coronaviruses, this critical step is governed by the virally-encoded spike (S) protein, a class I viral fusion protein that has several unique features. Coronavirus entry is unusual in that it is often biphasic in nature, and can occur at or near the cell surface or in late endosomes. Recent advances in structural, biochemical and molecular biology of the coronavirus S protein has shed light on the intricacies of coronavirus entry, in particular the molecular triggers of coronavirus S-mediated membrane fusion. Furthermore, characterization of the coronavirus fusion peptide (FP), the segment of the fusion protein that inserts to a target lipid bilayer during membrane fusion, has revealed its particular attributes which imparts some of the unusual properties of the S protein, such as Ca<sup>2+</sup>-dependency. These unusual characteristics can explain at least in part the biphasic nature of coronavirus entry. In this review, using severe acute respiratory syndrome coronavirus (SARS-CoV) as model virus, we give an overview of advances in research on the coronavirus fusion peptide with an emphasis on its role and properties within the biological context of host cell entry.</p></abstract><abstract abstract-type="author-highlights" id="ab0015"><title>Highlights</title><p><list list-type="simple" id="li0005"><list-item id="u0005"><label>•</label><p id="p0005">SARS-CoV as model for studying the coronavirus (CoV) fusion peptide (FP).</p></list-item><list-item id="u0010"><label>•</label><p id="p0010">Evidence based on functional and biophysical analyses that reveal the region downstream of the coronavirus spike protein S2′ cleavage as the <italic>bona fide</italic> FP that forms an extended “fusion platform”.</p></list-item><list-item id="u0015"><label>•</label><p id="p0015">Evidence for a direct role for calcium cations in mediating membrane fusion of SARS-CoV.</p></list-item><list-item id="u0020"><label>•</label><p id="p0020">Unusual features of the CoV FP that set it apart from other class I fusion peptides.</p></list-item><list-item id="u0025"><label>•</label><p id="p0025">The biphasic nature of SARS-CoV cellular entry pathways can be explained by calcium-dependency of fusion.</p></list-item></list></p></abstract><kwd-group id="keys0005"><title>Keywords</title><kwd>Coronavirus</kwd><kwd>SARS</kwd><kwd>Spike protein</kwd><kwd>Virus entry</kwd><kwd>Endosomes</kwd><kwd>Calcium</kwd><kwd>Fusion peptide</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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