Position-dependent processing of peptides presented on the surface of cowpea mosaic virus

The plant virus cowpea mosaic virus (CPMV) has been developed as an epitope -presentation system. Numerous epitopes have been expressed in the beta B-b eta C loop of the CPMV small coat protein, all of which undergo a cleavage reaction between their two carboxyterminal residues. Although many peptides presented in this manner give an authentic immune response, this was not t he case for the NIm-1A epitope from human rhinovirus-14. Crystallography re vealed significant differences between the structure of NIm-1A on CPMV comp ared with its native configuration. The 3D structure of CPMV expressing NIm -1A was used to design alterations to the context of the NIm-1A graft.