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Article: Quantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subunit

TitleQuantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subunit
Authors
KeywordsAntibodies
Cell-based receptor binding assay
SARS
Spike protein
Virus neutralization
Issue Date2006
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 2006, v. 580 n. 24, p. 5612-5620 How to Cite?
AbstractNeutralizing effects of antibodies targeting the C-terminal stalk (S2) subunit of the spike protein of severe acute respiratory syndrome coronavirus have previously been reported, although its mechanism remained elusive. In this study, high titered mouse antisera against the N-terminal globular (S1) and S2 subunits of the S protein were generated and total immunoglobulin G (IgG) was purified from these antisera. The efficiency of these purified IgGs in virus neutralization and blocking of receptor binding were compared quantitatively using virus neutralization assay and a previously developed cell-based receptor binding assay, respectively. We demonstrated that anti-S1 IgG neutralizes the virus and binds to the membrane associated S protein more efficiently than anti-S2 IgG does. Moreover, both anti-S1 and anti-S2 IgGs were able to abolish the binding between S protein and its cellular receptor(s), although anti-S1 IgG showed a significantly higher blocking efficiency. The unexpected blocking ability of anti-S2 IgG towards the receptor binding implied a possible role of the S2 subunit in virus docking process and argues against the current hypothesis of viral entry. On the other hand, the functional roles of the previously reported neutralizing epitopes within S2 subunit were investigated using an antigen specific antibody depletion assay. Depletion of antibodies against these regions significantly diminished, though not completely abolished, the neutralizing effects of anti-S2 IgG. It suggests the absence of a major neutralizing domain on S2 protein. The possible ways of anti-S2 IgGs to abolish the receptor binding and the factors restricting anti-S2 IgGs to neutralize the virus are discussed. © 2006.
Persistent Identifierhttp://hdl.handle.net/10722/78948
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorZeng, Fen_HK
dc.contributor.authorHon, CCen_HK
dc.contributor.authorYip, CWen_HK
dc.contributor.authorLaw, KMen_HK
dc.contributor.authorYeung, YSen_HK
dc.contributor.authorChan, KHen_HK
dc.contributor.authorMalik Peiris, JSen_HK
dc.contributor.authorLeung, FCCen_HK
dc.date.accessioned2010-09-06T07:48:45Z-
dc.date.available2010-09-06T07:48:45Z-
dc.date.issued2006en_HK
dc.identifier.citationFebs Letters, 2006, v. 580 n. 24, p. 5612-5620en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/78948-
dc.description.abstractNeutralizing effects of antibodies targeting the C-terminal stalk (S2) subunit of the spike protein of severe acute respiratory syndrome coronavirus have previously been reported, although its mechanism remained elusive. In this study, high titered mouse antisera against the N-terminal globular (S1) and S2 subunits of the S protein were generated and total immunoglobulin G (IgG) was purified from these antisera. The efficiency of these purified IgGs in virus neutralization and blocking of receptor binding were compared quantitatively using virus neutralization assay and a previously developed cell-based receptor binding assay, respectively. We demonstrated that anti-S1 IgG neutralizes the virus and binds to the membrane associated S protein more efficiently than anti-S2 IgG does. Moreover, both anti-S1 and anti-S2 IgGs were able to abolish the binding between S protein and its cellular receptor(s), although anti-S1 IgG showed a significantly higher blocking efficiency. The unexpected blocking ability of anti-S2 IgG towards the receptor binding implied a possible role of the S2 subunit in virus docking process and argues against the current hypothesis of viral entry. On the other hand, the functional roles of the previously reported neutralizing epitopes within S2 subunit were investigated using an antigen specific antibody depletion assay. Depletion of antibodies against these regions significantly diminished, though not completely abolished, the neutralizing effects of anti-S2 IgG. It suggests the absence of a major neutralizing domain on S2 protein. The possible ways of anti-S2 IgGs to abolish the receptor binding and the factors restricting anti-S2 IgGs to neutralize the virus are discussed. © 2006.en_HK
dc.languageengen_HK
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.rightsF E B S Letters. Copyright © Elsevier BV.en_HK
dc.subjectAntibodiesen_HK
dc.subjectCell-based receptor binding assayen_HK
dc.subjectSARSen_HK
dc.subjectSpike proteinen_HK
dc.subjectVirus neutralizationen_HK
dc.titleQuantitative comparison of the efficiency of antibodies against S1 and S2 subunit of SARS coronavirus spike protein in virus neutralization and blocking of receptor binding: Implications for the functional roles of S2 subuniten_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0014-5793&volume=580&spage=5612&epage=5620&date=2006&atitle=Quantitative+comparison+of+the+efficiency+of+antibodies+against+S1+and+S2+subunit+of+SARS+coronavirus+spike+protein+in+virus+neutralization+and+blocking+of+receptor+binding:+Implications+for+the+functional+roles+of+S2+subuniten_HK
dc.identifier.emailMalik Peiris, JS: malik@hkucc.hku.hken_HK
dc.identifier.emailLeung, FCC: fcleung@hkucc.hku.hken_HK
dc.identifier.authorityMalik Peiris, JS=rp00410en_HK
dc.identifier.authorityLeung, FCC=rp00731en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/j.febslet.2006.08.085en_HK
dc.identifier.pmid16989815en_HK
dc.identifier.scopuseid_2-s2.0-33749382628en_HK
dc.identifier.hkuros133453en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33749382628&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume580en_HK
dc.identifier.issue24en_HK
dc.identifier.spage5612en_HK
dc.identifier.epage5620en_HK
dc.identifier.isiWOS:000241461000002-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridZeng, F=7202911544en_HK
dc.identifier.scopusauthoridHon, CC=7003617137en_HK
dc.identifier.scopusauthoridYip, CW=7101665559en_HK
dc.identifier.scopusauthoridLaw, KM=7202563042en_HK
dc.identifier.scopusauthoridYeung, YS=9841205900en_HK
dc.identifier.scopusauthoridChan, KH=7406034307en_HK
dc.identifier.scopusauthoridMalik Peiris, JS=7005486823en_HK
dc.identifier.scopusauthoridLeung, FCC=7103078633en_HK

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