Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine
Identifieur interne : 000234 ( Pmc/Curation ); précédent : 000233; suivant : 000235Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine
Auteurs : Wanbo Tai [États-Unis] ; Lei He [République populaire de Chine] ; Xiujuan Zhang [États-Unis] ; Jing Pu [États-Unis, République populaire de Chine] ; Denis Voronin [États-Unis] ; Shibo Jiang [États-Unis, République populaire de Chine] ; Yusen Zhou [République populaire de Chine] ; Lanying Du [États-Unis]Source :
- Cellular and Molecular Immunology [ 1672-7681 ] ; 2020.
Abstract
The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.
Url:
DOI: 10.1038/s41423-020-0400-4
PubMed: NONE
PubMed Central: 7091888
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Kimball Research Institute,</institution><institution>New York Blood Center,</institution></institution-wrap>New York, NY USA</nlm:aff><country>États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>New York</wicri:cityArea></affiliation></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0442 2075</institution-id><institution-id institution-id-type="GRID">grid.250415.7</institution-id><institution>Lindsley F. Kimball Research Institute,</institution><institution>New York Blood Center,</institution></institution-wrap>New York, NY USA</nlm:aff><country>États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>New York</wicri:cityArea></affiliation><affiliation wicri:level="1"><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0125 2443</institution-id><institution-id institution-id-type="GRID">grid.8547.e</institution-id><institution>Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS),</institution><institution>School of Basic Medical Sciences, Fudan University,</institution></institution-wrap>Shanghai, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai</wicri:regionArea></affiliation></author><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name><affiliation wicri:level="1"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 8803 2373</institution-id><institution-id institution-id-type="GRID">grid.198530.6</institution-id><institution>Beijing Institute of Microbiology and Epidemiology,</institution></institution-wrap>Beijing, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Beijing</wicri:regionArea></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation wicri:level="2"><nlm:aff id="Aff1"><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0442 2075</institution-id><institution-id institution-id-type="GRID">grid.250415.7</institution-id><institution>Lindsley F. Kimball Research Institute,</institution><institution>New York Blood Center,</institution></institution-wrap>New York, NY USA</nlm:aff><country>États-Unis</country><placeName><region type="state">État de New York</region></placeName><wicri:cityArea>New York</wicri:cityArea></affiliation></author></analytic><series><title level="j">Cellular and Molecular Immunology</title><idno type="ISSN">1672-7681</idno><idno type="eISSN">2042-0226</idno><imprint><date when="2020">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="Par1">The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Du, L" uniqKey="Du L">L Du</name></author><author><name sortKey="He, Y" uniqKey="He Y">Y He</name></author><author><name sortKey="Zhou, Y" uniqKey="Zhou Y">Y Zhou</name></author><author><name sortKey="Liu, S" uniqKey="Liu S">S Liu</name></author><author><name sortKey="Zheng, Bj" uniqKey="Zheng B">BJ Zheng</name></author><author><name sortKey="Jiang, S" uniqKey="Jiang S">S Jiang</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Wang, N" uniqKey="Wang N">N Wang</name></author><author><name sortKey="Shang, J" uniqKey="Shang J">J Shang</name></author><author><name sortKey="Jiang, S" uniqKey="Jiang S">S Jiang</name></author><author><name sortKey="Du, L" uniqKey="Du L">L Du</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Zhong, Ns" uniqKey="Zhong N">NS Zhong</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zaki, Am" uniqKey="Zaki A">AM Zaki</name></author><author><name sortKey="Van Boheemen, S" uniqKey="Van Boheemen S">S van Boheemen</name></author><author><name sortKey="Bestebroer, Tm" uniqKey="Bestebroer T">TM Bestebroer</name></author><author><name sortKey="Osterhaus, Ad" uniqKey="Osterhaus A">AD Osterhaus</name></author><author><name sortKey="Fouchier, Ra" uniqKey="Fouchier R">RA Fouchier</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zhu, N" uniqKey="Zhu N">N Zhu</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Du, L" 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uniqKey="Du L">L Du</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tai, W" uniqKey="Tai W">W Tai</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chen, Wh" uniqKey="Chen W">WH Chen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chou, Tc" uniqKey="Chou T">TC Chou</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">Cell Mol Immunol</journal-id><journal-id journal-id-type="iso-abbrev">Cell. Mol. Immunol</journal-id><journal-title-group><journal-title>Cellular and Molecular Immunology</journal-title></journal-title-group><issn pub-type="ppub">1672-7681</issn><issn pub-type="epub">2042-0226</issn><publisher><publisher-name>Nature Publishing Group UK</publisher-name><publisher-loc>London</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmc">7091888</article-id><article-id pub-id-type="publisher-id">400</article-id><article-id pub-id-type="doi">10.1038/s41423-020-0400-4</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Tai</surname><given-names>Wanbo</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>He</surname><given-names>Lei</given-names></name><xref ref-type="aff" rid="Aff2">2</xref></contrib><contrib contrib-type="author"><name><surname>Zhang</surname><given-names>Xiujuan</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author"><name><surname>Pu</surname><given-names>Jing</given-names></name><xref ref-type="aff" rid="Aff1">1</xref><xref ref-type="aff" rid="Aff3">3</xref></contrib><contrib contrib-type="author"><contrib-id contrib-id-type="orcid">http://orcid.org/0000-0003-2652-0787</contrib-id><name><surname>Voronin</surname><given-names>Denis</given-names></name><xref ref-type="aff" rid="Aff1">1</xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Jiang</surname><given-names>Shibo</given-names></name><address><email>sjiang@nybc.org</email></address><xref ref-type="aff" rid="Aff1">1</xref><xref ref-type="aff" rid="Aff3">3</xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Zhou</surname><given-names>Yusen</given-names></name><address><email>yszhou@bmi.ac.cn</email></address><xref ref-type="aff" rid="Aff2">2</xref></contrib><contrib contrib-type="author" corresp="yes"><name><surname>Du</surname><given-names>Lanying</given-names></name><address><email>ldu@nybc.org</email></address><xref ref-type="aff" rid="Aff1">1</xref></contrib><aff id="Aff1"><label>1</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0004 0442 2075</institution-id><institution-id institution-id-type="GRID">grid.250415.7</institution-id><institution>Lindsley F. Kimball Research Institute,</institution><institution>New York Blood Center,</institution></institution-wrap>New York, NY USA</aff><aff id="Aff2"><label>2</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0000 8803 2373</institution-id><institution-id institution-id-type="GRID">grid.198530.6</institution-id><institution>Beijing Institute of Microbiology and Epidemiology,</institution></institution-wrap>Beijing, China</aff><aff id="Aff3"><label>3</label><institution-wrap><institution-id institution-id-type="ISNI">0000 0001 0125 2443</institution-id><institution-id institution-id-type="GRID">grid.8547.e</institution-id><institution>Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS),</institution><institution>School of Basic Medical Sciences, Fudan University,</institution></institution-wrap>Shanghai, China</aff></contrib-group><pub-date pub-type="epub"><day>19</day><month>3</month><year>2020</year></pub-date><pub-date pub-type="pmc-release"><day>19</day><month>3</month><year>2020</year></pub-date><fpage>1</fpage><lpage>8</lpage><history><date date-type="received"><day>3</day><month>3</month><year>2020</year></date><date date-type="accepted"><day>6</day><month>3</month><year>2020</year></date></history><permissions><copyright-statement>© CSI and USTC 2020</copyright-statement><license license-type="OpenAccess"><license-p><bold>Open Access</bold> This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">http://creativecommons.org/licenses/by/4.0/</ext-link>.</license-p></license></permissions><abstract id="Abs1"><p id="Par1">The outbreak of Coronavirus Disease 2019 (COVID-19) has posed a serious threat to global public health, calling for the development of safe and effective prophylactics and therapeutics against infection of its causative agent, severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), also known as 2019 novel coronavirus (2019-nCoV). The CoV spike (S) protein plays the most important roles in viral attachment, fusion and entry, and serves as a target for development of antibodies, entry inhibitors and vaccines. Here, we identified the receptor-binding domain (RBD) in SARS-CoV-2 S protein and found that the RBD protein bound strongly to human and bat angiotensin-converting enzyme 2 (ACE2) receptors. SARS-CoV-2 RBD exhibited significantly higher binding affinity to ACE2 receptor than SARS-CoV RBD and could block the binding and, hence, attachment of SARS-CoV-2 RBD and SARS-CoV RBD to ACE2-expressing cells, thus inhibiting their infection to host cells. SARS-CoV RBD-specific antibodies could cross-react with SARS-CoV-2 RBD protein, and SARS-CoV RBD-induced antisera could cross-neutralize SARS-CoV-2, suggesting the potential to develop SARS-CoV RBD-based vaccines for prevention of SARS-CoV-2 and SARS-CoV infection.</p></abstract><kwd-group xml:lang="en"><title>Keywords</title><kwd>2019 novel coronavirus</kwd><kwd>SARS-CoV-2</kwd><kwd>spike protein</kwd><kwd>receptor-binding domain</kwd><kwd>viral inhibitor</kwd><kwd>cross-neutralization</kwd></kwd-group><kwd-group kwd-group-type="npg-subject"><title>Subject terms</title><kwd>Viral infection</kwd><kwd>Immunotherapy</kwd></kwd-group><funding-group><award-group><funding-source><institution-wrap><institution-id institution-id-type="FundRef">https://doi.org/10.13039/100000002</institution-id><institution>U.S. Department of Health & Human Services | National Institutes of Health (NIH)</institution></institution-wrap></funding-source><award-id>R01AI137472</award-id><award-id>R01AI139092</award-id><principal-award-recipient><name><surname>Du</surname><given-names>Lanying</given-names></name></principal-award-recipient></award-group></funding-group><funding-group><award-group><funding-source><institution>U.S. Department of Health & Human Services | National Institutes of Health (NIH)</institution></funding-source></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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