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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Authors: | Szu-Chia?Lai Pele Choi-Sing?Chong Chia-Tsui?Yeh Levent Shih-Jen?Liu Jia-Tsrong?Jan Hsiang-Yun?Chi Hwan-Wun?Liu Ann?Chen Email author" target="_blank">Yeau-Ching?WangEmail author |
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Institution: | (1) Institute of Preventive Medicine, National Defense Medical Center, 90048-700, San-Hsia, Taipei, Taiwan;(2) Vaccine Research and Development Center, National Health Research Institutes, , Taiwan |
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Abstract: | Summary 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. |
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Keywords: | heptad repeat region monoclonal antibodies neutralizing epitope SARS-CoV spike protein |
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