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 betaB-betaC loop of the CPMV small coat protein, all of which undergo a cleavage reaction between their two carboxy-terminal 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 C PMV expressing NIm-1A was used to design alterations to the context of the NIm-1A graft.
Taylor
K M
KM
Dept. of Virus Research, John Innes Centre, Norwich, UK.
Porta
C
C
Lin
T
T
Johnson
J E
JE
Barker
P J
PJ
Lomonossoff
G P
GP
D000595:Amino Acid Sequence; D001483:Base Sequence; D002213:Capsid / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics; D036022:Capsid Proteins; D017798:Comovirus; D005822:Genetic Vectors; D006801:Humans; D008969:Molecular Sequence Data; D018532:Pisum sativum / Q000821:virology; D010455:Peptides; D011499:Protein Processing, Post-Translational; D012229:Rhinovirus / Q000737:chemistry* / Q000235:genetics
D036022:Capsid Proteins; D010455:Peptides