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Article: Antigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells
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TitleAntigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells
 
AuthorsDu, L3
Zhao, G1 2
Li, L3
He, Y3
Zhou, Y1
Zheng, BJ2
Jiang, S3
 
KeywordsAntigenicity
CHO cells
Immunogenicity
Receptor-binding domain
S protein
SARS-CoV
Stable expression
 
Issue Date2009
 
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
 
CitationBiochemical And Biophysical Research Communications, 2009, v. 384 n. 4, p. 486-490 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.bbrc.2009.05.003
 
AbstractThe receptor-binding domain (RBD) of SARS coronavirus (SARS-CoV) spike (S) protein contains multiple conformation-dependent epitopes that induce neutralizing antibody responses. Here we used CHO-K1 cells to establish a cell line for stable expression of a 193-mer (residues 318-510) RBD (RBD193-CHO) and determined its antigenicity and immunogenicity. We found that RBD193-CHO reacted strongly with a panel of six monoclonal antibodies recognizing various conformational and linear epitopes in RBD, suggesting that this recombinant protein maintains intact conformation and good antigenicity. Immunization of mice with RBD193-CHO resulted in induction of high titers of RBD-specific neutralizing antibodies and potent IL-4-expressing T cell responses. RBD193-CHO induced immunity that protected a majority of the vaccinated mice from SARS-CoV challenge. These results suggest that the recombinant RBD produced in an established stable cell line maintains strong immunogenicity with high potential for use as an effective and economic subunit SARS vaccine. © 2009 Elsevier Inc. All rights reserved.
 
ISSN0006-291X
2012 Impact Factor: 2.406
2012 SCImago Journal Rankings: 1.049
 
DOIhttp://dx.doi.org/10.1016/j.bbrc.2009.05.003
 
PubMed Central IDPMC2750803
 
ISI Accession Number IDWOS:000266689300017
 
ReferencesReferences in Scopus
 
DC FieldValue
dc.contributor.authorDu, L
 
dc.contributor.authorZhao, G
 
dc.contributor.authorLi, L
 
dc.contributor.authorHe, Y
 
dc.contributor.authorZhou, Y
 
dc.contributor.authorZheng, BJ
 
dc.contributor.authorJiang, S
 
dc.date.accessioned2010-10-31T11:12:28Z
 
dc.date.available2010-10-31T11:12:28Z
 
dc.date.issued2009
 
dc.description.abstractThe receptor-binding domain (RBD) of SARS coronavirus (SARS-CoV) spike (S) protein contains multiple conformation-dependent epitopes that induce neutralizing antibody responses. Here we used CHO-K1 cells to establish a cell line for stable expression of a 193-mer (residues 318-510) RBD (RBD193-CHO) and determined its antigenicity and immunogenicity. We found that RBD193-CHO reacted strongly with a panel of six monoclonal antibodies recognizing various conformational and linear epitopes in RBD, suggesting that this recombinant protein maintains intact conformation and good antigenicity. Immunization of mice with RBD193-CHO resulted in induction of high titers of RBD-specific neutralizing antibodies and potent IL-4-expressing T cell responses. RBD193-CHO induced immunity that protected a majority of the vaccinated mice from SARS-CoV challenge. These results suggest that the recombinant RBD produced in an established stable cell line maintains strong immunogenicity with high potential for use as an effective and economic subunit SARS vaccine. © 2009 Elsevier Inc. All rights reserved.
 
dc.description.naturelink_to_OA_fulltext
 
dc.identifier.citationBiochemical And Biophysical Research Communications, 2009, v. 384 n. 4, p. 486-490 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.bbrc.2009.05.003
 
dc.identifier.doihttp://dx.doi.org/10.1016/j.bbrc.2009.05.003
 
dc.identifier.epage490
 
dc.identifier.hkuros175095
 
dc.identifier.isiWOS:000266689300017
 
dc.identifier.issn0006-291X
2012 Impact Factor: 2.406
2012 SCImago Journal Rankings: 1.049
 
dc.identifier.issue4
 
dc.identifier.openurl
 
dc.identifier.pmcidPMC2750803
 
dc.identifier.pmid19422787
 
dc.identifier.scopuseid_2-s2.0-65649110128
 
dc.identifier.spage486
 
dc.identifier.urihttp://hdl.handle.net/10722/125119
 
dc.identifier.volume384
 
dc.languageeng
 
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/wps/find/journaldescription.cws_home/622790/description
 
dc.publisher.placeUnited States
 
dc.relation.ispartofBiochemical and Biophysical Research Communications
 
dc.relation.referencesReferences in Scopus
 
dc.subject.meshAnimals
 
dc.subject.meshAntibodies, Viral - biosynthesis
 
dc.subject.meshMembrane Glycoproteins - biosynthesis - immunology
 
dc.subject.meshSARS Virus - immunology
 
dc.subject.meshViral Envelope Proteins - biosynthesis - immunology
 
dc.subjectAntigenicity
 
dc.subjectCHO cells
 
dc.subjectImmunogenicity
 
dc.subjectReceptor-binding domain
 
dc.subjectS protein
 
dc.subjectSARS-CoV
 
dc.subjectStable expression
 
dc.titleAntigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells
 
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