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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
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TitleRecombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity
 
AuthorsDu, L3
Zhao, G1 2
Chan, CCS2
Sun, S1
Chen, M2
Liu, Z3
Guo, H3
He, Y3
Zhou, Y1
Zheng, BJ2
Jiang, S3
 
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
 
CitationVirology, 2009, v. 393 n. 1, p. 144-150 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.virol.2009.07.018
 
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.
 
ISSN0042-6822
2012 Impact Factor: 3.367
2012 SCImago Journal Rankings: 1.428
 
DOIhttp://dx.doi.org/10.1016/j.virol.2009.07.018
 
PubMed Central IDPMC2753736
 
ISI Accession Number IDWOS:000270453600018
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).

 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorDu, L
 
dc.contributor.authorZhao, G
 
dc.contributor.authorChan, CCS
 
dc.contributor.authorSun, S
 
dc.contributor.authorChen, M
 
dc.contributor.authorLiu, Z
 
dc.contributor.authorGuo, H
 
dc.contributor.authorHe, Y
 
dc.contributor.authorZhou, Y
 
dc.contributor.authorZheng, BJ
 
dc.contributor.authorJiang, S
 
dc.date.accessioned2010-10-31T11:13:26Z
 
dc.date.available2010-10-31T11:13:26Z
 
dc.date.issued2009
 
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.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationVirology, 2009, v. 393 n. 1, p. 144-150 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.virol.2009.07.018
 
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dc.identifier.doihttp://dx.doi.org/10.1016/j.virol.2009.07.018
 
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dc.identifier.isiWOS:000270453600018
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).

 
dc.identifier.issn0042-6822
2012 Impact Factor: 3.367
2012 SCImago Journal Rankings: 1.428
 
dc.identifier.issue1
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC2753736
 
dc.identifier.pmid19683779
 
dc.identifier.scopuseid_2-s2.0-70349383960
 
dc.identifier.spage144
 
dc.identifier.urihttp://hdl.handle.net/10722/125136
 
dc.identifier.volume393
 
dc.languageeng
 
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yviro
 
dc.publisher.placeUnited States
 
dc.relation.ispartofVirology
 
dc.relation.referencesReferences in Scopus
 
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.subjectNeutralizing antibody
 
dc.subjectProtective immunity
 
dc.subjectReceptor-binding domain
 
dc.subjectSARS-CoV
 
dc.subjectSubunit vaccines
 
dc.titleRecombinant receptor-binding domain of SARS-CoV spike protein expressed in mammalian, insect and E. coli cells elicits potent neutralizing antibody and protective immunity
 
dc.typeArticle
 
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Author Affiliations
  1. Institute of Microbiology Chinese Academy of Sciences
  2. The University of Hong Kong
  3. New York Blood Center