Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus

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The sudden emergence of severe acute respiratory syndrome (SARS) at the end of 2002 resultedin 774 reported deaths from more than 8000 cases worldwide. As no effective vaccines or antiviralagents are available, the most effective measure to prevent the expansion of a SARS epidemicis the rapid diagnosis and isolation of SARS patients. To establish specific diagnosticmethods, we generated nine clones of monoclonal antibodies to nucleocapsid protein (NP) ofSARS-coronavirus (SARS-CoV). On immunofluorescent antibody assay and Western blottinganalysis, none of the monoclonal antibodies showed cross-reactivity to authentic and recombinantNPs of human coronavirus (HCoV) 229E strain. To determine the region on the NP moleculewhere the monoclonal antibodies bind, we generated four truncated recombinant NPs andanalyzed the reactivity between monoclonal antibodies and truncated NPs. Two monoclonalantibodies reacted with a truncated NP covering from amino acid residues 111 to 230, andseven reacted with another truncated NP covering from amino acid residues 221 to 340. Epitopemapping analysis indicated that monoclonal antibody SN5-25 recognized the amino acidsequence Q^{245}TVTKK^{250} on SARS-NP. Within the epitope, Q245, T246, V247, K249, and K250 appearedto form an essential motif for monoclonal antibody SN5-25 to bind. The informationabout binding sites and epitopes of monoclonal antibodies may be useful for the developmentof new diagnostic methods for SARS and for analyzing the function of N protein of SARS-CoV.
2008-03-07

Characterization and epitope mapping of monoclonal antibodies to the nucleocapsid protein of severe acute respiratory syndrome coronavirus

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