Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine.
Identifieur interne : 002B23 ( PubMed/Corpus ); précédent : 002B22; suivant : 002B24Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine.
Auteurs : Yuxian He ; Yusen Zhou ; Shuwen Liu ; Zhihua Kou ; Wenhui Li ; Michael Farzan ; Shibo JiangSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
English descriptors
- KwdEn :
- Animals, Antibodies (chemistry), Cell Line, Dose-Response Relationship, Immunologic, Enzyme-Linked Immunosorbent Assay, Flow Cytometry, Humans, Immunoglobulin Fragments (chemistry), Immunoglobulin G (chemistry), Membrane Glycoproteins (chemistry), Plasmids (metabolism), Protein Structure, Tertiary, Rabbits, Recombinant Fusion Proteins (chemistry), Spike Glycoprotein, Coronavirus, Vaccines (chemistry), Viral Envelope Proteins (chemistry).
- MESH :
- chemical , chemistry : Antibodies, Immunoglobulin Fragments, Immunoglobulin G, Membrane Glycoproteins, Recombinant Fusion Proteins, Vaccines, Viral Envelope Proteins.
- metabolism : Plasmids.
- Animals, Cell Line, Dose-Response Relationship, Immunologic, Enzyme-Linked Immunosorbent Assay, Flow Cytometry, Humans, Protein Structure, Tertiary, Rabbits, Spike Glycoprotein, Coronavirus.
Abstract
The spike (S) protein of severe acute respiratory syndrome (SARS) coronavirus (CoV), a type I transmembrane envelope glycoprotein, consists of S1 and S2 domains responsible for virus binding and fusion, respectively. The S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. Here we show that a recombinant fusion protein (designated RBD-Fc) containing 193-amino acid RBD (residues 318-510) and a human IgG1 Fc fragment can induce highly potent antibody responses in the immunized rabbits. The antibodies recognized RBD on S1 domain and completely inhibited SARS-CoV infection at a serum dilution of 1:10,240. Rabbit antisera effectively blocked binding of S1, which contains RBD, to ACE2. This suggests that RBD can induce highly potent neutralizing antibody responses and has potential to be developed as an effective and safe subunit vaccine for prevention of SARS.
DOI: 10.1016/j.bbrc.2004.09.106
PubMed: 15474494
Links to Exploration step
pubmed:15474494Le document en format XML
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Kimball Research Institute, New York Blood Center, New York, NY 10021, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name></author><author><name sortKey="Liu, Shuwen" sort="Liu, Shuwen" uniqKey="Liu S" first="Shuwen" last="Liu">Shuwen Liu</name></author><author><name sortKey="Kou, Zhihua" sort="Kou, Zhihua" uniqKey="Kou Z" first="Zhihua" last="Kou">Zhihua Kou</name></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2004">2004</date><idno type="RBID">pubmed:15474494</idno><idno type="pmid">15474494</idno><idno type="doi">10.1016/j.bbrc.2004.09.106</idno><idno type="wicri:Area/PubMed/Corpus">002B23</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002B23</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine.</title><author><name sortKey="He, Yuxian" sort="He, Yuxian" uniqKey="He Y" first="Yuxian" last="He">Yuxian He</name><affiliation><nlm:affiliation>Viral Immunology Laboratory, Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name></author><author><name sortKey="Liu, Shuwen" sort="Liu, Shuwen" uniqKey="Liu S" first="Shuwen" last="Liu">Shuwen Liu</name></author><author><name sortKey="Kou, Zhihua" sort="Kou, Zhihua" uniqKey="Kou Z" first="Zhihua" last="Kou">Zhihua Kou</name></author><author><name sortKey="Li, Wenhui" sort="Li, Wenhui" uniqKey="Li W" first="Wenhui" last="Li">Wenhui Li</name></author><author><name sortKey="Farzan, Michael" sort="Farzan, Michael" uniqKey="Farzan M" first="Michael" last="Farzan">Michael Farzan</name></author><author><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Antibodies (chemistry)</term><term>Cell Line</term><term>Dose-Response Relationship, Immunologic</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Flow Cytometry</term><term>Humans</term><term>Immunoglobulin Fragments (chemistry)</term><term>Immunoglobulin G (chemistry)</term><term>Membrane Glycoproteins (chemistry)</term><term>Plasmids (metabolism)</term><term>Protein Structure, Tertiary</term><term>Rabbits</term><term>Recombinant Fusion Proteins (chemistry)</term><term>Spike Glycoprotein, Coronavirus</term><term>Vaccines (chemistry)</term><term>Viral Envelope Proteins (chemistry)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antibodies</term><term>Immunoglobulin Fragments</term><term>Immunoglobulin G</term><term>Membrane Glycoproteins</term><term>Recombinant Fusion Proteins</term><term>Vaccines</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Plasmids</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Dose-Response Relationship, Immunologic</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Flow Cytometry</term><term>Humans</term><term>Protein Structure, Tertiary</term><term>Rabbits</term><term>Spike Glycoprotein, Coronavirus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The spike (S) protein of severe acute respiratory syndrome (SARS) coronavirus (CoV), a type I transmembrane envelope glycoprotein, consists of S1 and S2 domains responsible for virus binding and fusion, respectively. The S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. Here we show that a recombinant fusion protein (designated RBD-Fc) containing 193-amino acid RBD (residues 318-510) and a human IgG1 Fc fragment can induce highly potent antibody responses in the immunized rabbits. The antibodies recognized RBD on S1 domain and completely inhibited SARS-CoV infection at a serum dilution of 1:10,240. Rabbit antisera effectively blocked binding of S1, which contains RBD, to ACE2. This suggests that RBD can induce highly potent neutralizing antibody responses and has potential to be developed as an effective and safe subunit vaccine for prevention of SARS.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15474494</PMID><DateCompleted><Year>2004</Year><Month>12</Month><Day>20</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>324</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Nov</Month><Day>12</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>Receptor-binding domain of SARS-CoV spike protein induces highly potent neutralizing antibodies: implication for developing subunit vaccine.</ArticleTitle><Pagination><MedlinePgn>773-81</MedlinePgn></Pagination><Abstract><AbstractText>The spike (S) protein of severe acute respiratory syndrome (SARS) coronavirus (CoV), a type I transmembrane envelope glycoprotein, consists of S1 and S2 domains responsible for virus binding and fusion, respectively. The S1 contains a receptor-binding domain (RBD) that can specifically bind to angiotensin-converting enzyme 2 (ACE2), the receptor on target cells. Here we show that a recombinant fusion protein (designated RBD-Fc) containing 193-amino acid RBD (residues 318-510) and a human IgG1 Fc fragment can induce highly potent antibody responses in the immunized rabbits. The antibodies recognized RBD on S1 domain and completely inhibited SARS-CoV infection at a serum dilution of 1:10,240. Rabbit antisera effectively blocked binding of S1, which contains RBD, to ACE2. This suggests that RBD can induce highly potent neutralizing antibody responses and has potential to be developed as an effective and safe subunit vaccine for prevention of SARS.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>He</LastName><ForeName>Yuxian</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Viral Immunology Laboratory, Lindsley F. 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UI="D004797" MajorTopicYN="N">Enzyme-Linked Immunosorbent Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005434" MajorTopicYN="N">Flow Cytometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007128" MajorTopicYN="N">Immunoglobulin Fragments</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007074" MajorTopicYN="N">Immunoglobulin G</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName><QualifierName UI="Q000378" 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