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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

TitleAntibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitro
Authors
KeywordsADE
Protection
SARS-CoV
Issue Date2007
PublisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/vaccine
Citation
Vaccine, 2007, v. 25 n. 4, p. 729-740 How to Cite?
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 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.
Persistent Identifierhttp://hdl.handle.net/10722/78808
ISSN
2013 Impact Factor: 3.485
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKam, YWen_HK
dc.contributor.authorKien, Fen_HK
dc.contributor.authorRoberts, Aen_HK
dc.contributor.authorCheung, YCen_HK
dc.contributor.authorLamirande, EWen_HK
dc.contributor.authorVogel, Len_HK
dc.contributor.authorChu, SLen_HK
dc.contributor.authorTse, Jen_HK
dc.contributor.authorGuarner, Jen_HK
dc.contributor.authorZaki, SRen_HK
dc.contributor.authorSubbarao, Ken_HK
dc.contributor.authorPeiris, Men_HK
dc.contributor.authorNal, Ben_HK
dc.contributor.authorAltmeyer, Ren_HK
dc.date.accessioned2010-09-06T07:47:04Z-
dc.date.available2010-09-06T07:47:04Z-
dc.date.issued2007en_HK
dc.identifier.citationVaccine, 2007, v. 25 n. 4, p. 729-740en_HK
dc.identifier.issn0264-410Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/78808-
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.en_HK
dc.languageengen_HK
dc.publisherElsevier Ltd. The Journal's web site is located at http://www.elsevier.com/locate/vaccineen_HK
dc.relation.ispartofVaccineen_HK
dc.subjectADEen_HK
dc.subjectProtectionen_HK
dc.subjectSARS-CoVen_HK
dc.titleAntibodies against trimeric S glycoprotein protect hamsters against SARS-CoV challenge despite their capacity to mediate FcγRII-dependent entry into B cells in vitroen_HK
dc.typeArticleen_HK
dc.identifier.emailPeiris, M: malik@hkucc.hku.hken_HK
dc.identifier.emailNal, B: bnal@hkucc.hku.hken_HK
dc.identifier.authorityPeiris, M=rp00410en_HK
dc.identifier.authorityNal, B=rp00541en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.vaccine.2006.08.011en_HK
dc.identifier.pmid17049691en_HK
dc.identifier.scopuseid_2-s2.0-33845227481en_HK
dc.identifier.hkuros134712en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33845227481&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume25en_HK
dc.identifier.issue4en_HK
dc.identifier.spage729en_HK
dc.identifier.epage740en_HK
dc.identifier.isiWOS:000243741900019-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridKam, YW=15122219300en_HK
dc.identifier.scopusauthoridKien, F=7004231633en_HK
dc.identifier.scopusauthoridRoberts, A=7404498719en_HK
dc.identifier.scopusauthoridCheung, YC=15121975000en_HK
dc.identifier.scopusauthoridLamirande, EW=6602826730en_HK
dc.identifier.scopusauthoridVogel, L=7102142468en_HK
dc.identifier.scopusauthoridChu, SL=15121933900en_HK
dc.identifier.scopusauthoridTse, J=36928243100en_HK
dc.identifier.scopusauthoridGuarner, J=7004588460en_HK
dc.identifier.scopusauthoridZaki, SR=7101848151en_HK
dc.identifier.scopusauthoridSubbarao, K=7102213212en_HK
dc.identifier.scopusauthoridPeiris, M=7005486823en_HK
dc.identifier.scopusauthoridNal, B=6506672380en_HK
dc.identifier.scopusauthoridAltmeyer, R=7003677186en_HK

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