SrasV1, PubMed, Curation, bibRecord, 001223

Immunogenicity and protection efficacy of monomeric and trimeric recombinant SARS coronavirus spike protein subunit vaccine candidates.

Identifieur interne : 001223 ( PubMed/Curation ); précédent : 001222; suivant : 001224

Immunogenicity and protection efficacy of monomeric and trimeric recombinant SARS coronavirus spike protein subunit vaccine candidates.

Auteurs : Jie Li [États-Unis] ; Laura Ulitzky ; Erica Silberstein ; Deborah R. Taylor ; Raphael Viscidi

Source :

Viral immunology [ 1557-8976 ] ; 2013.

RBID : pubmed:23573979

Descripteurs français

English descriptors

KwdEn :
- Animals, Antibodies, Neutralizing (blood), Antibodies, Viral (blood), Antigens, Viral (genetics), Antigens, Viral (immunology), Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Membrane Glycoproteins (genetics), Membrane Glycoproteins (immunology), Mice, Mice, Inbred BALB C, Neutralization Tests, Protein Folding, Protein Structure, Tertiary, Recombinant Proteins (genetics), Recombinant Proteins (immunology), SARS Virus (genetics), SARS Virus (immunology), Severe Acute Respiratory Syndrome (prevention & control), Spike Glycoprotein, Coronavirus, Survival Analysis, Vaccines, Subunit (administration & dosage), Vaccines, Subunit (immunology), Vaccines, Synthetic (administration & dosage), Vaccines, Synthetic (immunology), Viral Envelope Proteins (genetics), Viral Envelope Proteins (immunology), Viral Vaccines (administration & dosage), Viral Vaccines (immunology).
MESH :
- chemical , administration & dosage : Vaccines, Subunit, Vaccines, Synthetic, Viral Vaccines.
- chemical , blood : Antibodies, Neutralizing, Antibodies, Viral.
- chemical , genetics : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Viral Envelope Proteins.
- chemical , immunology : Antigens, Viral, Membrane Glycoproteins, Recombinant Proteins, Vaccines, Subunit, Vaccines, Synthetic, Viral Envelope Proteins, Viral Vaccines.
- genetics : SARS Virus.
- immunology : SARS Virus.
- prevention & control : Severe Acute Respiratory Syndrome.
- Animals, Disease Models, Animal, Enzyme-Linked Immunosorbent Assay, Mice, Mice, Inbred BALB C, Neutralization Tests, Protein Folding, Protein Structure, Tertiary, Spike Glycoprotein, Coronavirus, Survival Analysis.

Abstract

Severe acute respiratory syndrome (SARS) is a newly emerging infectious disease, and an effective vaccine is not available. In this study, we compared the immunogenicity and protection efficacy of recombinant proteins corresponding to different domains of the SARS-coronavirus spike protein. Trimeric recombinant proteins were created by fusing the foldon domain derived from T4 bacteriophage to the carboxy-termini of individual domains of the spike protein. While the full-length ectodomain (S) of the spike protein, the full-length ectodomain fused to foldon (S-foldon), the S1 domain (S1), S1-foldon, and the S2 domain(S2) antigens all elicited comparable antibody titers as measured by ELISA, S-foldon induced a significantly higher titer of neutralizing antibody and S2 protein did not elicit virus neutralizing antibodies. When tested in a mouse virus replication model, all the mice vaccinated with the S1, S1-foldon, S, or S-foldon were completely protected.

DOI: 10.1089/vim.2012.0076
PubMed: 23573979

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Le document en format XML

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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome (SARS) is a newly emerging infectious disease, and an effective vaccine is not available. In this study, we compared the immunogenicity and protection efficacy of recombinant proteins corresponding to different domains of the SARS-coronavirus spike protein. Trimeric recombinant proteins were created by fusing the foldon domain derived from T4 bacteriophage to the carboxy-termini of individual domains of the spike protein. While the full-length ectodomain (S) of the spike protein, the full-length ectodomain fused to foldon (S-foldon), the S1 domain (S1), S1-foldon, and the S2 domain(S2) antigens all elicited comparable antibody titers as measured by ELISA, S-foldon induced a significantly higher titer of neutralizing antibody and S2 protein did not elicit virus neutralizing antibodies. When tested in a mouse virus replication model, all the mice vaccinated with the S1, S1-foldon, S, or S-foldon were completely protected.</div>
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Immunogenicity and protection efficacy of monomeric and trimeric recombinant SARS coronavirus spike protein subunit vaccine candidates.

Immunogenicity and protection efficacy of monomeric and trimeric recombinant SARS coronavirus spike protein subunit vaccine candidates.

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