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Article: Recombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity

TitleRecombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity
Authors
KeywordsNeutralizing antibody
Protective immunity
Receptor-binding domain
SARS-CoV
Subunit vaccines
Issue Date2009
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
Citation
Virology, 2009, v. 393 n. 1, p. 144-150 How to Cite?
AbstractSevere acute respiratory syndrome (SARS) is a newly emerging infectious disease. The potential recurrence of the disease from animal reservoirs highlights the significance of development of safe and efficient vaccines to prevent a future SARS epidemic. In this study, we expressed the recombinant receptor-binding domain (rRBD) in mammalian (293T) cells, insect (Sf9) cells, and E. coli, respectively, and compared their immunogenicity and protection against SARS-CoV infection in an established mouse model. Our results show that all rRBD proteins expressed in the above systems maintained intact conformation, being able to induce highly potent neutralizing antibody responses and complete protective immunity against SARS-CoV challenge in mice, albeit the rRBD expressed in 293T cells elicited stronger humoral immune responses with significantly higher neutralizing activity (P < 0.05) than those expressed in Sf9 and E. coli cells. These results suggest that all three rRBDs are effective in eliciting immune responses and protection against SARS-CoV and any of the above expression systems can be used for production of rRBD-based SARS subunit vaccines. Preference will be given to rRBD expressed in mammalian cells for future evaluation of the vaccine efficacy in a non-human primate model of SARS because of its ability to refold into a native conformation more readily and to induce higher level of neutralizing antibody responses than those expressed in E. coli and insect cells. © 2009 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/125136
ISSN
2023 Impact Factor: 2.8
2023 SCImago Journal Rankings: 0.838
PubMed Central ID
ISI Accession Number ID
Funding AgencyGrant Number
National Institutes of Health (NIH) of the United StatesR01 AI68002
Control of Infectious Diseases, the Health, Welfare and Food Bureau of the Hong Kong SAR Government
National 973 Basic Research Program of China2005CB523001
Funding Information:

This study was supported by the National Institutes of Health (NIH) of the United States (R01 AI68002), by the Research Fund for the Control of Infectious Diseases, the Health, Welfare and Food Bureau of the Hong Kong SAR Government, and by the National 973 Basic Research Program of China (2005CB523001).

References

 

DC FieldValueLanguage
dc.contributor.authorDu, Len_HK
dc.contributor.authorZhao, Gen_HK
dc.contributor.authorChan, CCSen_HK
dc.contributor.authorSun, Sen_HK
dc.contributor.authorChen, Men_HK
dc.contributor.authorLiu, Zen_HK
dc.contributor.authorGuo, Hen_HK
dc.contributor.authorHe, Yen_HK
dc.contributor.authorZhou, Yen_HK
dc.contributor.authorZheng, BJen_HK
dc.contributor.authorJiang, Sen_HK
dc.date.accessioned2010-10-31T11:13:26Z-
dc.date.available2010-10-31T11:13:26Z-
dc.date.issued2009en_HK
dc.identifier.citationVirology, 2009, v. 393 n. 1, p. 144-150en_HK
dc.identifier.issn0042-6822en_HK
dc.identifier.urihttp://hdl.handle.net/10722/125136-
dc.description.abstractSevere acute respiratory syndrome (SARS) is a newly emerging infectious disease. The potential recurrence of the disease from animal reservoirs highlights the significance of development of safe and efficient vaccines to prevent a future SARS epidemic. In this study, we expressed the recombinant receptor-binding domain (rRBD) in mammalian (293T) cells, insect (Sf9) cells, and E. coli, respectively, and compared their immunogenicity and protection against SARS-CoV infection in an established mouse model. Our results show that all rRBD proteins expressed in the above systems maintained intact conformation, being able to induce highly potent neutralizing antibody responses and complete protective immunity against SARS-CoV challenge in mice, albeit the rRBD expressed in 293T cells elicited stronger humoral immune responses with significantly higher neutralizing activity (P < 0.05) than those expressed in Sf9 and E. coli cells. These results suggest that all three rRBDs are effective in eliciting immune responses and protection against SARS-CoV and any of the above expression systems can be used for production of rRBD-based SARS subunit vaccines. Preference will be given to rRBD expressed in mammalian cells for future evaluation of the vaccine efficacy in a non-human primate model of SARS because of its ability to refold into a native conformation more readily and to induce higher level of neutralizing antibody responses than those expressed in E. coli and insect cells. © 2009 Elsevier Inc. All rights reserved.en_HK
dc.languageengen_HK
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviroen_HK
dc.relation.ispartofVirologyen_HK
dc.subjectNeutralizing antibodyen_HK
dc.subjectProtective immunityen_HK
dc.subjectReceptor-binding domainen_HK
dc.subjectSARS-CoVen_HK
dc.subjectSubunit vaccinesen_HK
dc.subject.meshAntibodies, Viral - blood-
dc.subject.meshMembrane Glycoproteins - genetics - immunology-
dc.subject.meshSARS Virus - genetics - immunology-
dc.subject.meshSevere Acute Respiratory Syndrome - immunology - prevention and control-
dc.subject.meshViral Envelope Proteins - genetics - immunology-
dc.titleRecombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunityen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0042-6822&volume=393&issue=1&spage=144&epage=150&date=2009&atitle=Recombinant+receptor-binding+domain+of+SARS-CoV+spike+protein+expressed+in+mammalian,+insect+and+E.+coli+cells+elicits+potent+neutralizing+antibody+and+protective+immunityen_HK
dc.identifier.emailZheng, BJ:bzheng@hkucc.hku.hken_HK
dc.identifier.authorityZheng, BJ=rp00353en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1016/j.virol.2009.07.018en_HK
dc.identifier.pmid19683779-
dc.identifier.pmcidPMC2753736-
dc.identifier.scopuseid_2-s2.0-70349383960en_HK
dc.identifier.hkuros175097en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-70349383960&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume393en_HK
dc.identifier.issue1en_HK
dc.identifier.spage144en_HK
dc.identifier.epage150en_HK
dc.identifier.isiWOS:000270453600018-
dc.publisher.placeUnited Statesen_HK
dc.identifier.f10001728969-
dc.identifier.scopusauthoridDu, L=8686996200en_HK
dc.identifier.scopusauthoridZhao, G=8684553000en_HK
dc.identifier.scopusauthoridChan, CCS=36984586600en_HK
dc.identifier.scopusauthoridSun, S=35171536200en_HK
dc.identifier.scopusauthoridChen, M=7406353413en_HK
dc.identifier.scopusauthoridLiu, Z=16319107300en_HK
dc.identifier.scopusauthoridGuo, H=23667379800en_HK
dc.identifier.scopusauthoridHe, Y=8742157400en_HK
dc.identifier.scopusauthoridZhou, Y=8791655300en_HK
dc.identifier.scopusauthoridZheng, BJ=7201780588en_HK
dc.identifier.scopusauthoridJiang, S=7404453146en_HK
dc.identifier.citeulike5475713-
dc.identifier.issnl0042-6822-

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