Two distinct linear epitopes were identified on the FCV VP1 capsid surface: a highly conserved epitope recognized by non-neutralizing MAbs and a highly variable epitope recognized by neutralizing MAbs.
The identification of highly conserved non-neutralizing and highly variable neutralizing epitopes on the FCV capsid provides valuable tools for diagnostic applications and understanding viral infection mechanisms.
We report the generation, characterization and epitope mapping of a panel of 26 monoclonal antibodies (MAbs) against the VP1 capsid protein of feline calicivirus (FCV). Two close but distinct linear epitopes were identified at the capsid outermost surface (P2 subdomain) of VP1, within the E5'HVR antigenic hypervariable region: one spanning amino acids 431-435 (PAGDY), highly conserved and recognized by non-neutralizing MAbs; and a second epitope spanning amino acids 445-451 (ITTANQY), highly variable and recognized by neutralizing MAbs. These antibodies might be valuable for diagnostic applications, as well as for further research in different aspects of the biology of FCV.
Cubillos‐Zapata et al. (Fri,) conducted a other in Feline calicivirus (FCV). Monoclonal antibodies against FCV VP1 was evaluated on Epitope mapping of monoclonal antibodies. Two distinct linear epitopes were identified on the FCV VP1 capsid surface: a highly conserved epitope recognized by non-neutralizing MAbs and a highly variable epitope recognized by neutralizing MAbs.