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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, A2
Cheung, YC1
Lamirande, EW2
Vogel, L2
Chu, SL3
Tse, J3
Guarner, J5
Zaki, SR5
Subbarao, K2
Peiris, M1
Nal, B3
Altmeyer, R4
 
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
2012 Impact Factor: 3.492
2012 SCImago Journal Rankings: 1.360
 
DOIhttp://dx.doi.org/10.1016/j.vaccine.2006.08.011
 
ISI Accession Number IDWOS:000243741900019
 
ReferencesReferences in Scopus
 
DC FieldValue
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
2012 Impact Factor: 3.492
2012 SCImago Journal Rankings: 1.360
 
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
 
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<contributor.author>Chu, SL</contributor.author>
<contributor.author>Tse, J</contributor.author>
<contributor.author>Guarner, J</contributor.author>
<contributor.author>Zaki, SR</contributor.author>
<contributor.author>Subbarao, K</contributor.author>
<contributor.author>Peiris, M</contributor.author>
<contributor.author>Nal, B</contributor.author>
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Author Affiliations
  1. The University of Hong Kong
  2. National Institute of Allergy and Infectious Diseases
  3. HKU-Pasteur Research Centre
  4. CombinatoRx Singapore Ltd.
  5. Centers for Disease Control and Prevention