SrasV1, Ncbi, Merge, bibRecord, 001F09

Antigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells.

Identifieur interne : 001F09 ( Ncbi/Merge ); précédent : 001F08; suivant : 001F10

Antigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells.

Auteurs : Lanying Du [États-Unis] ; Guangyu Zhao ; Lin Li ; Yuxian He ; Yusen Zhou ; Bo-Jian Zheng ; Shibo Jiang

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2009.

RBID : pubmed:19422787

Descripteurs français

English descriptors

KwdEn :
- Animals, Antibodies, Viral (biosynthesis), CHO Cells, Cricetinae, Cricetulus, Female, Interleukin-4 (immunology), Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (immunology), Mice, Mice, Inbred BALB C, Protein Structure, Tertiary, Receptors, Virus (immunology), SARS Virus (immunology), Severe Acute Respiratory Syndrome (prevention & control), Spike Glycoprotein, Coronavirus, T-Lymphocytes (immunology), Vaccination, Viral Envelope Proteins (biosynthesis), Viral Envelope Proteins (immunology).
MESH :
- chemical , biosynthesis : Antibodies, Viral, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : Interleukin-4, Membrane Glycoproteins, Receptors, Virus, Viral Envelope Proteins.
- immunology : SARS Virus, T-Lymphocytes.
- prevention & control : Severe Acute Respiratory Syndrome.
- Animals, CHO Cells, Cricetinae, Cricetulus, Female, Mice, Mice, Inbred BALB C, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Vaccination.

Abstract

The 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.

DOI: 10.1016/j.bbrc.2009.05.003
PubMed: 19422787

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The 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.</div>
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<name sortKey="Zhao, Guangyu" sort="Zhao, Guangyu" uniqKey="Zhao G" first="Guangyu" last="Zhao">Guangyu Zhao</name>
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Antigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells.

Antigenicity and immunogenicity of SARS-CoV S protein receptor-binding domain stably expressed in CHO cells.

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