Immunogenicity of a receptor-binding domain of SARS coronavirus spike protein in mice : Implications for a subunit vaccine
Identifieur interne : 000571 ( PascalFrancis/Curation ); précédent : 000570; suivant : 000572Immunogenicity of a receptor-binding domain of SARS coronavirus spike protein in mice : Implications for a subunit vaccine
Auteurs : Alexander N. Zakhartchouk [Canada] ; Chetna Sharon [Canada] ; Malathy Satkunarajah [Canada] ; Thierry Auperin [Canada] ; Sathiyanarayanan Viswanathan [Canada] ; George Mutwiri [Canada] ; Martin Petric [Canada] ; Raymond H. See [Canada] ; Robert C. Brunham [Canada] ; B. Brett Finlay [Canada] ; Cheryl Cameron [Canada] ; David J. Kelvin [Canada] ; Alan Cochrane [Canada] ; James M. Rini [Canada] ; Lorne A. Babiuk [Canada]Source :
- Vaccine [ 0264-410X ] ; 2007.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Vaccin.
English descriptors
Abstract
We studied the immunogenicity of an anti-SARS subunit vaccine comprised of the fragment of the SARS coronavirus (SARS-CoV) spike protein amino acids 318-510 (S318-510) containing the receptor-binding domain. The S protein fragment was purified from the culture supernatant of stably transformed HEK293T cells secreting a tagged version of the protein. The vaccine was given subcutaneously to 129S6/SvEv mice in saline, with alum adjuvant or with alum plus CpG oligodeoxynucleotides (ODN). Mice immunized with the adjuvanted antigen elicited strong antibody and cellular immune responses; furthermore, adding the CpG ODN to the alum resulted in increased IgG2a antibody titers and a higher number of INF-γ-secreting murine splenocytes. Mice vaccinated with S318-510 deglycosylated by PNGase F (dgS318-510) showed a lower neutralizing antibody response but had similar numbers of INF-γ-producing cells in the spleen. This finding suggests that carbohydrate is important for the immunogenicity of the S318-510 protein fragment and provide useful information for designing an effective and safe SARS subunit vaccine.
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a">Immunogenicity of a receptor-binding domain of SARS coronavirus spike protein in mice : Implications for a subunit vaccine</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Immunogenicity</term>
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<term>Vaccine</term>
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<term>Souris</term>
<term>Immunogénicité</term>
<term>Protéine</term>
<term>Sousunité</term>
<term>Vaccin</term>
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<front><div type="abstract" xml:lang="en">We studied the immunogenicity of an anti-SARS subunit vaccine comprised of the fragment of the SARS coronavirus (SARS-CoV) spike protein amino acids 318-510 (S318-510) containing the receptor-binding domain. The S protein fragment was purified from the culture supernatant of stably transformed HEK293T cells secreting a tagged version of the protein. The vaccine was given subcutaneously to 129S6/SvEv mice in saline, with alum adjuvant or with alum plus CpG oligodeoxynucleotides (ODN). Mice immunized with the adjuvanted antigen elicited strong antibody and cellular immune responses; furthermore, adding the CpG ODN to the alum resulted in increased IgG2a antibody titers and a higher number of INF-γ-secreting murine splenocytes. Mice vaccinated with S318-510 deglycosylated by PNGase F (dgS318-510) showed a lower neutralizing antibody response but had similar numbers of INF-γ-producing cells in the spleen. This finding suggests that carbohydrate is important for the immunogenicity of the S318-510 protein fragment and provide useful information for designing an effective and safe SARS subunit vaccine.</div>
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