Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.
Identifieur interne : 002013 ( PubMed/Corpus ); précédent : 002012; suivant : 002014Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcgammaRII-dependent entry into B cells in vitro.
Auteurs : Yiu Wing Kam ; François Kien ; Anjeanette Roberts ; Yan Chung Cheung ; Elaine W. Lamirande ; Leatrice Vogel ; Shui Ling Chu ; Jane Tse ; Jeannette Guarner ; Sherif R. Zaki ; Kanta Subbarao ; Malik Peiris ; Béatrice Nal ; Ralf AltmeyerSource :
- Vaccine [ 0264-410X ] ; 2007.
English descriptors
- KwdEn :
- Animals, Antibodies, Viral (immunology), B-Lymphocytes (metabolism), Cricetinae, Dose-Response Relationship, Drug, Immunity, Mucosal, Immunoglobulin A (metabolism), Immunoglobulin G (metabolism), Membrane Glycoproteins (immunology), Mice, Receptors, IgG (metabolism), SARS Virus (immunology), Severe Acute Respiratory Syndrome (prevention & control), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (immunology).
- MESH :
- chemical , immunology : Antibodies, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- immunology : SARS Virus.
- metabolism : B-Lymphocytes, Immunoglobulin A, Immunoglobulin G, Receptors, IgG.
- prevention & control : Severe Acute Respiratory Syndrome.
- Animals, Cricetinae, Dose-Response Relationship, Drug, Immunity, Mucosal, Mice, Spike Glycoprotein, Coronavirus.
Abstract
Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.
DOI: 10.1016/j.vaccine.2006.08.011
PubMed: 17049691
Links to Exploration step
pubmed:17049691Le document en format XML
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<front><div type="abstract" xml:lang="en">Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.</div>
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<Abstract><AbstractText>Vaccine-induced antibodies can prevent or, in the case of feline infectious peritonitis virus, aggravate infections by coronaviruses. We investigated whether a recombinant native full-length S-protein trimer (triSpike) of severe acute respiratory syndrome coronavirus (SARS-CoV) was able to elicit a neutralizing and protective immune response in animals and analyzed the capacity of anti-S antibodies to mediate antibody-dependent enhancement (ADE) of virus entry in vitro and enhancement of replication in vivo. SARS-CoV-specific serum and mucosal immunoglobulins were readily detected in immunized animals. Serum IgG blocked binding of the S-protein to the ACE2 receptor and neutralized SARS-CoV infection in vitro. Entry into human B cell lines occurred in a FcgammaRII-dependent and ACE2-independent fashion indicating that ADE of virus entry is a novel cell entry mechanism of SARS-CoV. Vaccinated animals showed no signs of enhanced lung pathology or hepatitis and viral load was undetectable or greatly reduced in lungs following challenge with SARS-CoV. Altogether our results indicate that a recombinant trimeric S protein was able to elicit an efficacious protective immune response in vivo and warrant concern in the safety evaluation of a human vaccine against SARS-CoV.</AbstractText>
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