Peptide display on Potato virus X: Molecular features of the coat protein-fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles

Chiara Lico, Floriana Capuano, Giovanni Renzone, Marcello Donini, Carla Marusic, Andrea Scaloni, Eugenio Benvenuto, Selene Baschieri

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

The potexvirus Potato virus X(PVX) can be modified genetically to generate chimeric virus particles (CVPS) carrying heterologous peptides fused to coat protein (CP) subunits. A spontaneous PVX mutant expressing a truncated, but functional, form of the CP has been isolated. With the aim of exploiting this virus to display peptides useful for vaccine formulations, two novel viral expression vectors based on pPVX201 (bearing the wild-type PVX genome) were constructed encoding the truncated CP. Both vectors were able to produce infectious virus particles in planta and were used to insert a panel of sequences encoding pepticles of biopharmaceutical interest as N-terminal fusions to the truncated cp gene. The analysis of infection progression induced by the different constructs enabled identification of two important structural features of the fused peptide, namely tryptophan content and isoelectric point, critically affecting the formation of PVX CVPs and virus movement through the plant. These results are discussed in view of the rising interest in engineered plant viruses for development of peptide-based epitope vaccines. © 2006 SGM.
Original languageEnglish
Pages (from-to)3103 - 3112
Number of pages10
JournalJournal of General Virology
Volume87
Issue number10
DOIs
Publication statusPublished - Oct 2006
Externally publishedYes

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Virology
  • Immunology

Cite this