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 : 000094 ( PubMed/Corpus ); précédent : 000093; suivant : 000095Characterization 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 ; Lei He ; Xiujuan Zhang ; Jing Pu ; Denis Voronin ; Shibo Jiang ; Yusen Zhou ; Lanying DuSource :
- Cellular & molecular immunology [ 2042-0226 ] ; 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.
DOI: 10.1038/s41423-020-0400-4
PubMed: 32203189
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Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Pu, Jing" sort="Pu, Jing" uniqKey="Pu J" first="Jing" last="Pu">Jing Pu</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Voronin, Denis" sort="Voronin, Denis" uniqKey="Voronin D" first="Denis" last="Voronin">Denis Voronin</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. sjiang@nybc.org.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name><affiliation><nlm:affiliation>Beijing Institute of Microbiology and Epidemiology, Beijing, China. yszhou@bmi.ac.cn.</nlm:affiliation></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation><nlm:affiliation>Lindsley F. 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Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="He, Lei" sort="He, Lei" uniqKey="He L" first="Lei" last="He">Lei He</name><affiliation><nlm:affiliation>Beijing Institute of Microbiology and Epidemiology, Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Zhang, Xiujuan" sort="Zhang, Xiujuan" uniqKey="Zhang X" first="Xiujuan" last="Zhang">Xiujuan Zhang</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Pu, Jing" sort="Pu, Jing" uniqKey="Pu J" first="Jing" last="Pu">Jing Pu</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Voronin, Denis" sort="Voronin, Denis" uniqKey="Voronin D" first="Denis" last="Voronin">Denis Voronin</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. sjiang@nybc.org.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name><affiliation><nlm:affiliation>Beijing Institute of Microbiology and Epidemiology, Beijing, China. yszhou@bmi.ac.cn.</nlm:affiliation></affiliation></author><author><name sortKey="Du, Lanying" sort="Du, Lanying" uniqKey="Du L" first="Lanying" last="Du">Lanying Du</name><affiliation><nlm:affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. ldu@nybc.org.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Cellular & molecular immunology</title><idno type="eISSN">2042-0226</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">32203189</PMID><DateRevised><Year>2020</Year><Month>03</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">2042-0226</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Mar</Month><Day>19</Day></PubDate></JournalIssue><Title>Cellular & molecular immunology</Title><ISOAbbreviation>Cell. Mol. Immunol.</ISOAbbreviation></Journal><ArticleTitle>Characterization of the receptor-binding domain (RBD) of 2019 novel coronavirus: implication for development of RBD protein as a viral attachment inhibitor and vaccine.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41423-020-0400-4</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tai</LastName><ForeName>Wanbo</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>He</LastName><ForeName>Lei</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Beijing Institute of Microbiology and Epidemiology, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Xiujuan</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pu</LastName><ForeName>Jing</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Voronin</LastName><ForeName>Denis</ForeName><Initials>D</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-2652-0787</Identifier><AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Shibo</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. sjiang@nybc.org.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Key Laboratory of Medical Molecular Virology (MOE/NHC/CAMS), School of Basic Medical Sciences, Fudan University, Shanghai, China. sjiang@nybc.org.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zhou</LastName><ForeName>Yusen</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Beijing Institute of Microbiology and Epidemiology, Beijing, China. yszhou@bmi.ac.cn.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Du</LastName><ForeName>Lanying</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY, USA. ldu@nybc.org.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01AI137472</GrantID><Agency>U.S. Department of Health & Human Services | National Institutes of Health (NIH)</Agency><Country></Country></Grant><Grant><GrantID>R01AI139092</GrantID><Agency>U.S. Department of Health & Human Services | National Institutes of Health (NIH)</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>03</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>China</Country><MedlineTA>Cell Mol Immunol</MedlineTA><NlmUniqueID>101242872</NlmUniqueID><ISSNLinking>1672-7681</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">2019 novel coronavirus</Keyword><Keyword MajorTopicYN="N">SARS-CoV-2</Keyword><Keyword MajorTopicYN="N">cross-neutralization</Keyword><Keyword MajorTopicYN="N">receptor-binding domain</Keyword><Keyword MajorTopicYN="N">spike protein</Keyword><Keyword MajorTopicYN="N">viral inhibitor</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2020</Year><Month>03</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>03</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>3</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>3</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>3</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32203189</ArticleId><ArticleId IdType="doi">10.1038/s41423-020-0400-4</ArticleId><ArticleId IdType="pii">10.1038/s41423-020-0400-4</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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