SrasV1, PubMed, Curation, bibRecord, 002562

Characterization of neutralizing monoclonal antibodies recognizing a 15-residues epitope on the spike protein HR2 region of severe acute respiratory syndrome coronavirus (SARS-CoV).

Identifieur interne : 002562 ( PubMed/Curation ); précédent : 002561; suivant : 002563

Characterization of neutralizing monoclonal antibodies recognizing a 15-residues epitope on the spike protein HR2 region of severe acute respiratory syndrome coronavirus (SARS-CoV).

Auteurs : Szu-Chia Lai [Taïwan] ; Pele Choi-Sing Chong ; Chia-Tsui Yeh ; Levent Shih-Jen Liu ; Jia-Tsrong Jan ; Hsiang-Yun Chi ; Hwan-Wun Liu ; Ann Chen ; Yeau-Ching Wang

Source :

Journal of biomedical science [ 1021-7770 ] ; 2005.

RBID : pubmed:16132115

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal (chemistry), Antibodies, Monoclonal (immunology), Base Sequence, Blotting, Western, DNA Primers, Electrophoretic Mobility Shift Assay, Enzyme-Linked Immunosorbent Assay, Epitopes (chemistry), Epitopes (immunology), Fluorescent Antibody Technique, Indirect, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (immunology), Mice, Mice, Inbred BALB C, Molecular Sequence Data, Neutralization Tests, SARS Virus (immunology), Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (immunology).
MESH :
- chemical , chemistry : Antibodies, Monoclonal, Epitopes, Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , immunology : Antibodies, Monoclonal, Epitopes, Membrane Glycoproteins, Viral Envelope Proteins.
- immunology : SARS Virus.
- Amino Acid Sequence, Animals, Base Sequence, Blotting, Western, DNA Primers, Electrophoretic Mobility Shift Assay, Enzyme-Linked Immunosorbent Assay, Fluorescent Antibody Technique, Indirect, Mice, Mice, Inbred BALB C, Molecular Sequence Data, Neutralization Tests, Spike Glycoprotein, Coronavirus.

Abstract

The spike (S) glycoprotein is thought to play a complex and central role in the biology and pathogenesis of SARS coronavirus infection. In this study, a recombinant protein (rS268, corresponding to residues 268-1255 of SARS-CoV S protein) was expressed in Escherichia coli and was purified to near homogeneity. After immunization with rS268, S protein-specific BALB/c antisera and mAbs were induced and confirmed using ELISA, Western blot and IFA. Several BALB/c mAbs were found to be effectively to neutralize the infection of Vero E6 cells by SARS-CoV in a dose-dependent manner. Systematic epitope mapping showed that all these neutralizing mAbs recognized a 15-residues peptide (CB-119) corresponding to residues 1143-1157 (SPDVDLGDISGINAS) that was located to the second heptad repeat (HR2) region of the SARS-CoV spike protein. The peptide CB-119 could specifically inhibit the interaction of neutralizing mAbs and spike protein in a dose-dependent manner. Further, neutralizing mAbs, but not control mAbs, could specifically interact with CB-119 in a dose-dependent manner. Results implicated that the second heptad repeat region of spike protein could be a good target for vaccine development against SARS-CoV.

DOI: 10.1007/s11373-005-9004-3
PubMed: 16132115

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Le document en format XML

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<front><div type="abstract" xml:lang="en">The spike (S) glycoprotein is thought to play a complex and central role in the biology and pathogenesis of SARS coronavirus infection. In this study, a recombinant protein (rS268, corresponding to residues 268-1255 of SARS-CoV S protein) was expressed in Escherichia coli and was purified to near homogeneity. After immunization with rS268, S protein-specific BALB/c antisera and mAbs were induced and confirmed using ELISA, Western blot and IFA. Several BALB/c mAbs were found to be effectively to neutralize the infection of Vero E6 cells by SARS-CoV in a dose-dependent manner. Systematic epitope mapping showed that all these neutralizing mAbs recognized a 15-residues peptide (CB-119) corresponding to residues 1143-1157 (SPDVDLGDISGINAS) that was located to the second heptad repeat (HR2) region of the SARS-CoV spike protein. The peptide CB-119 could specifically inhibit the interaction of neutralizing mAbs and spike protein in a dose-dependent manner. Further, neutralizing mAbs, but not control mAbs, could specifically interact with CB-119 in a dose-dependent manner. Results implicated that the second heptad repeat region of spike protein could be a good target for vaccine development against SARS-CoV.</div>
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<Abstract><AbstractText>The spike (S) glycoprotein is thought to play a complex and central role in the biology and pathogenesis of SARS coronavirus infection. In this study, a recombinant protein (rS268, corresponding to residues 268-1255 of SARS-CoV S protein) was expressed in Escherichia coli and was purified to near homogeneity. After immunization with rS268, S protein-specific BALB/c antisera and mAbs were induced and confirmed using ELISA, Western blot and IFA. Several BALB/c mAbs were found to be effectively to neutralize the infection of Vero E6 cells by SARS-CoV in a dose-dependent manner. Systematic epitope mapping showed that all these neutralizing mAbs recognized a 15-residues peptide (CB-119) corresponding to residues 1143-1157 (SPDVDLGDISGINAS) that was located to the second heptad repeat (HR2) region of the SARS-CoV spike protein. The peptide CB-119 could specifically inhibit the interaction of neutralizing mAbs and spike protein in a dose-dependent manner. Further, neutralizing mAbs, but not control mAbs, could specifically interact with CB-119 in a dose-dependent manner. Results implicated that the second heptad repeat region of spike protein could be a good target for vaccine development against SARS-CoV.</AbstractText>
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Characterization of neutralizing monoclonal antibodies recognizing a 15-residues epitope on the spike protein HR2 region of severe acute respiratory syndrome coronavirus (SARS-CoV).

Characterization of neutralizing monoclonal antibodies recognizing a 15-residues epitope on the spike protein HR2 region of severe acute respiratory syndrome coronavirus (SARS-CoV).

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