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

Biol Chem. 1999 Mar;380(3):387-92. doi: 10.1515/BC.1999.051.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Capsid / biosynthesis
  • Capsid / chemistry*
  • Capsid / genetics
  • Capsid Proteins
  • Comovirus*
  • Genetic Vectors*
  • Humans
  • Molecular Sequence Data
  • Peptides
  • Pisum sativum / virology
  • Protein Processing, Post-Translational*
  • Rhinovirus / chemistry*
  • Rhinovirus / genetics

Substances

  • Capsid Proteins
  • Peptides