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
2011 Impact Factor: 2.484
2011 SCImago Journal Rankings: 0.287
DOIhttp://dx.doi.org/10.1016/j.bbrc.2009.05.003
ISI Accession Number IDWOS:000266689300017
PubMed Central IDPMC2750803
ReferencesReferences in Scopus
DC Field
Value
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
2011 Impact Factor: 2.484
2011 SCImago Journal Rankings: 0.287
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
Author Affiliations
  1. Institute of Microbiology Chinese Academy of Sciences
  2. The University of Hong Kong
  3. New York Blood Center