Inactivated SARS-CoV vaccine elicits high titers of spike protein-specific antibodies that block receptor binding and virus entry
Identifieur interne : 005293 ( Main/Exploration ); précédent : 005292; suivant : 005294Inactivated 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 [République populaire de Chine] ; Pamela Siddiqui [États-Unis] ; Shibo Jiang [États-Unis]Source :
- 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 β-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.
Url:
DOI: 10.1016/j.bbrc.2004.10.052
PubMed: 15530413
PubMed Central: 7092874
Affiliations:
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Le document en format XML
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Kimball Research Institute, New York Blood Center, New York, NY 10021, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Viral Immunology Laboratory, Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></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">Department of Molecular Biology, Beijing Institute of Microbiology and Epidemiology, Beijing 100071, China</nlm:aff><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Department of Molecular Biology, Beijing Institute of Microbiology and Epidemiology, Beijing 100071</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Siddiqui, Pamela" sort="Siddiqui, Pamela" uniqKey="Siddiqui P" first="Pamela" last="Siddiqui">Pamela Siddiqui</name><affiliation wicri:level="2"><nlm:aff id="aff1">Viral Immunology Laboratory, Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Viral Immunology Laboratory, Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021</wicri:regionArea><placeName><region type="state">État de New York</region></placeName></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">Viral Immunology Laboratory, Lindsley F. Kimball Research Institute, New York Blood Center, New York, NY 10021, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Viral Immunology Laboratory, Lindsley F. 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l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (immunologie)</term><term>Protéines recombinantes ()</term><term>Protéines recombinantes (génétique)</term><term>Protéines recombinantes (immunologie)</term><term>Récepteurs viraux (immunologie)</term><term>Récepteurs viraux (métabolisme)</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Structure tertiaire des protéines</term><term>Sérums immuns (immunologie)</term><term>Test ELISA</term><term>Vaccins antiviraux (immunologie)</term><term>Vaccins antiviraux (pharmacologie)</term><term>Vaccins inactivés (immunologie)</term><term>Virus du SRAS (immunologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Antibodies, Viral</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Antibodies, Viral</term><term>Antiviral Agents</term><term>Immune Sera</term><term>Receptors, Virus</term><term>Recombinant Proteins</term><term>Vaccines, Inactivated</term><term>Viral Envelope Proteins</term><term>Viral Vaccines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxypeptidases</term><term>Receptors, Virus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antiviral Agents</term><term>Viral Vaccines</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Anticorps antiviraux</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines de l'enveloppe virale</term><term>Protéines 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Tertiary</term><term>Rabbits</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Lapins</term><term>Liaison aux protéines</term><term>Peptidyl-Dipeptidase A</term><term>Protéines de l'enveloppe virale</term><term>Protéines recombinantes</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Structure tertiaire des protéines</term><term>Test ELISA</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>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 β-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.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Drosten, C" uniqKey="Drosten C">C. Drosten</name></author><author><name sortKey="Gunther, S" uniqKey="Gunther S">S. Gunther</name></author><author><name sortKey="Preiser, W" uniqKey="Preiser W">W. Preiser</name></author><author><name sortKey="Van Der, W S" uniqKey="Van Der W">W.S. van der</name></author><author><name sortKey="Brodt, H R" uniqKey="Brodt H">H.R. Brodt</name></author><author><name sortKey="Becker, S" uniqKey="Becker S">S. Becker</name></author><author><name sortKey="Rabenau, H" uniqKey="Rabenau H">H. 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Lu</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>République populaire de Chine</li><li>États-Unis</li></country><region><li>État de New York</li></region><settlement><li>Pékin</li></settlement></list><tree><country name="États-Unis"><region name="État de New York"><name sortKey="He, Yuxian" sort="He, Yuxian" uniqKey="He Y" first="Yuxian" last="He">Yuxian He</name></region><name sortKey="Jiang, Shibo" sort="Jiang, Shibo" uniqKey="Jiang S" first="Shibo" last="Jiang">Shibo Jiang</name><name sortKey="Siddiqui, Pamela" sort="Siddiqui, Pamela" uniqKey="Siddiqui P" first="Pamela" last="Siddiqui">Pamela Siddiqui</name></country><country name="République populaire de Chine"><noRegion><name sortKey="Zhou, Yusen" sort="Zhou, Yusen" uniqKey="Zhou Y" first="Yusen" last="Zhou">Yusen Zhou</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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