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Position-Dependent Processing of Peptides Presented on the Surface of Cowpea Mosaic Virus

Abstract The plant virus cowpea mosaic virus (CPMV) has been developed as an epitope-presentation system. Numerous epitopes have been expressed in the βB-βC 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 the case for the NIm-1A epitope from human rhinovirus-14. Crystallography revealed significant differences between the structure of NIm-1A on CPMV compared 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.