Inactivated SARS-CoV vaccine elicits high titers of spike protein-specific antibodies that block receptor binding and virus entry.
Identifieur interne : 002A58 ( PubMed/Curation ); précédent : 002A57; suivant : 002A59Inactivated SARS-CoV vaccine elicits high titers of spike protein-specific antibodies that block receptor binding and virus entry.
Auteurs : Yuxian He [États-Unis] ; Yusen Zhou ; Pamela Siddiqui ; Shibo JiangSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2004.
Descripteurs français
- KwdFr :
- Animaux, Anticorps antiviraux (biosynthèse), Anticorps antiviraux (immunologie), Antiviraux (immunologie), Antiviraux (pharmacologie), Carboxypeptidases (métabolisme), Lapins, Liaison aux protéines, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (immunologie), Protéines recombinantes (), Protéines recombinantes (génétique), Protéines recombinantes (immunologie), Récepteurs viraux (immunologie), Récepteurs viraux (métabolisme), Souris, Souris de lignée BALB C, Structure tertiaire des protéines, Sérums immuns (immunologie), Test ELISA, Vaccins antiviraux (immunologie), Vaccins antiviraux (pharmacologie), Vaccins inactivés (immunologie), Virus du SRAS (immunologie).
- MESH :
- biosynthèse : Anticorps antiviraux.
- génétique : Protéines de l'enveloppe virale, Protéines recombinantes.
- immunologie : Anticorps antiviraux, Antiviraux, Protéines de l'enveloppe virale, Protéines recombinantes, Récepteurs viraux, Sérums immuns, Vaccins antiviraux, Vaccins inactivés, Virus du SRAS.
- métabolisme : Carboxypeptidases, Récepteurs viraux.
- pharmacologie : Antiviraux, Vaccins antiviraux.
- Animaux, Lapins, Liaison aux protéines, Peptidyl-Dipeptidase A, Protéines de l'enveloppe virale, Protéines recombinantes, Souris, Souris de lignée BALB C, Structure tertiaire des protéines, Test ELISA.
English descriptors
- KwdEn :
- Animals, Antibodies, Viral (biosynthesis), Antibodies, Viral (immunology), Antiviral Agents (immunology), Antiviral Agents (pharmacology), Carboxypeptidases (metabolism), Enzyme-Linked Immunosorbent Assay, Immune Sera (immunology), Mice, Mice, Inbred BALB C, Peptidyl-Dipeptidase A, Protein Binding, Protein Structure, Tertiary, Rabbits, Receptors, Virus (immunology), Receptors, Virus (metabolism), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Recombinant Proteins (immunology), SARS Virus (immunology), Vaccines, Inactivated (immunology), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Vaccines (immunology), Viral Vaccines (pharmacology).
- MESH :
- chemical , biosynthesis : Antibodies, Viral.
- chemical , chemistry : Recombinant Proteins, Viral Envelope Proteins.
- chemical , genetics : Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Viral, Antiviral Agents, Immune Sera, Receptors, Virus, Recombinant Proteins, Vaccines, Inactivated, Viral Envelope Proteins, Viral Vaccines.
- chemical , metabolism : Carboxypeptidases, Receptors, Virus.
- chemical , pharmacology : Antiviral Agents, Viral Vaccines.
- immunology : SARS Virus.
- Animals, Enzyme-Linked Immunosorbent Assay, Mice, Mice, Inbred BALB C, Peptidyl-Dipeptidase A, Protein Binding, Protein Structure, Tertiary, Rabbits.
Abstract
The only severe acute respiratory syndrome (SARS) vaccine currently being tested in clinical trial consists of inactivated severe acute respiratory syndrome-associate coronavirus (SARS-CoV). However, limited information is available about host immune responses induced by the inactivated SARS vaccine. In this study, we demonstrated that SARS-CoV inactivated by beta-propiolactone elicited high titers of antibodies in the immunized mice and rabbits that recognize the spike (S) protein, especially the receptor-binding domain (RBD) in the S1 region. The antisera from the immunized animals efficiently bound to the RBD and blocked binding of RBD to angiotensin-converting enzyme 2, the functional receptor on the susceptible cells for SARS-CoV. With a sensitive and quantitative single-cycle infection assay using pseudovirus bearing the SARS-CoV S protein, we demonstrated that mouse and rabbit antisera significantly inhibited S protein-mediated virus entry with mean 50% inhibitory titers of 1:7393 and 1:2060, respectively. These data suggest that the RBD of S protein is a major neutralization determinant in the inactivated SARS vaccine which can induce potent neutralizing antibodies to block SARS-CoV entry. However, caution should be taken in using the inactivated SARS-CoV as a vaccine since it may also cause harmful immune and/or inflammatory responses.
DOI: 10.1016/j.bbrc.2004.10.052
PubMed: 15530413
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However, limited information is available about host immune responses induced by the inactivated SARS vaccine. In this study, we demonstrated that SARS-CoV inactivated by beta-propiolactone elicited high titers of antibodies in the immunized mice and rabbits that recognize the spike (S) protein, especially the receptor-binding domain (RBD) in the S1 region. The antisera from the immunized animals efficiently bound to the RBD and blocked binding of RBD to angiotensin-converting enzyme 2, the functional receptor on the susceptible cells for SARS-CoV. With a sensitive and quantitative single-cycle infection assay using pseudovirus bearing the SARS-CoV S protein, we demonstrated that mouse and rabbit antisera significantly inhibited S protein-mediated virus entry with mean 50% inhibitory titers of 1:7393 and 1:2060, respectively. These data suggest that the RBD of S protein is a major neutralization determinant in the inactivated SARS vaccine which can induce potent neutralizing antibodies to block SARS-CoV entry. However, caution should be taken in using the inactivated SARS-CoV as a vaccine since it may also cause harmful immune and/or inflammatory responses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15530413</PMID><DateCompleted><Year>2005</Year><Month>02</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>31</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>325</Volume><Issue>2</Issue><PubDate><Year>2004</Year><Month>Dec</Month><Day>10</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem. Biophys. Res. Commun.</ISOAbbreviation></Journal><ArticleTitle>Inactivated SARS-CoV vaccine elicits high titers of spike protein-specific antibodies that block receptor binding and virus entry.</ArticleTitle><Pagination><MedlinePgn>445-52</MedlinePgn></Pagination><Abstract><AbstractText>The only severe acute respiratory syndrome (SARS) vaccine currently being tested in clinical trial consists of inactivated severe acute respiratory syndrome-associate coronavirus (SARS-CoV). However, limited information is available about host immune responses induced by the inactivated SARS vaccine. In this study, we demonstrated that SARS-CoV inactivated by beta-propiolactone elicited high titers of antibodies in the immunized mice and rabbits that recognize the spike (S) protein, especially the receptor-binding domain (RBD) in the S1 region. The antisera from the immunized animals efficiently bound to the RBD and blocked binding of RBD to angiotensin-converting enzyme 2, the functional receptor on the susceptible cells for SARS-CoV. With a sensitive and quantitative single-cycle infection assay using pseudovirus bearing the SARS-CoV S protein, we demonstrated that mouse and rabbit antisera significantly inhibited S protein-mediated virus entry with mean 50% inhibitory titers of 1:7393 and 1:2060, respectively. These data suggest that the RBD of S protein is a major neutralization determinant in the inactivated SARS vaccine which can induce potent neutralizing antibodies to block SARS-CoV entry. However, caution should be taken in using the inactivated SARS-CoV as a vaccine since it may also cause harmful immune and/or inflammatory responses.</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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MajorTopicYN="N">Rabbits</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011991" MajorTopicYN="N">Receptors, Virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015164" MajorTopicYN="N">Vaccines, Inactivated</DescriptorName><QualifierName UI="Q000276" 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