Article: Antibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro

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TitleAntibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro
AuthorsKam, YW3
Kien, F3
Roberts, A4
Cheung, YC1
Lamirande, EW4
Vogel, L4
Chu, SL3
Tse, J3
Guarner, J5
Zaki, SR5
Subbarao, K4
Peiris, M1
Nal, B3
Altmeyer, R2
KeywordsADE
Protection
SARS-CoV
Issue Date2007
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/vaccine
CitationVaccine, 2007, v. 25 n. 4, p. 729-740 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.vaccine.2006.08.011
AbstractVaccine-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 FcγRII-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. © 2006 Elsevier Ltd. All rights reserved.
ISSN0264-410X
2011 Impact Factor: 3.766
2011 SCImago Journal Rankings: 0.369
DOIhttp://dx.doi.org/10.1016/j.vaccine.2006.08.011
ISI Accession Number IDWOS:000243741900019
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorKam, YW
dc.contributor.authorKien, F
dc.contributor.authorRoberts, A
dc.contributor.authorCheung, YC
dc.contributor.authorLamirande, EW
dc.contributor.authorVogel, L
dc.contributor.authorChu, SL
dc.contributor.authorTse, J
dc.contributor.authorGuarner, J
dc.contributor.authorZaki, SR
dc.contributor.authorSubbarao, K
dc.contributor.authorPeiris, M
dc.contributor.authorNal, B
dc.contributor.authorAltmeyer, R
dc.date.accessioned2010-09-06T07:47:04Z
dc.date.available2010-09-06T07:47:04Z
dc.date.issued2007
dc.description.abstractVaccine-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 FcγRII-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. © 2006 Elsevier Ltd. All rights reserved.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationVaccine, 2007, v. 25 n. 4, p. 729-740 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.vaccine.2006.08.011
dc.identifier.doihttp://dx.doi.org/10.1016/j.vaccine.2006.08.011
dc.identifier.epage740
dc.identifier.hkuros134712
dc.identifier.isiWOS:000243741900019
dc.identifier.issn0264-410X
2011 Impact Factor: 3.766
2011 SCImago Journal Rankings: 0.369
dc.identifier.issue4
dc.identifier.pmid17049691
dc.identifier.scopuseid_2-s2.0-33845227481
dc.identifier.spage729
dc.identifier.urihttp://hdl.handle.net/10722/78808
dc.identifier.volume25
dc.languageeng
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/vaccine
dc.publisher.placeUnited Kingdom
dc.relation.ispartofVaccine
dc.relation.referencesReferences in Scopus
dc.subjectADE
dc.subjectProtection
dc.subjectSARS-CoV
dc.titleAntibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro
dc.typeArticle
Author Affiliations
  1. The University of Hong Kong
  2. CombinatoRx Singapore Ltd.
  3. HKU-Pasteur Research Centre
  4. National Institute of Allergy and Infectious Diseases
  5. Centers for Disease Control and Prevention