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

Journal of Biomedical Science
Szu-Chia LaiYeau-Ching Wang

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.

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Feb 10, 2009·Nature Reviews. Microbiology·Lanying DuShibo Jiang
May 18, 2007·Biochemical and Biophysical Research Communications·Shu-Pei LienShih-Jen Liu
May 16, 2006·Journal of Structural Biology·Brian TripetRobert S Hodges
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Mar 31, 2021·Virology Journal·Zachary A KrummYuxing Xia
Jun 16, 2021·Genome Medicine·Christof C SmithAlex Rubinsteyn

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