PhiXing-it, displaying foreign peptides on bacteriophage ΦX174

Kristofer J. Christakos, Janice A. Chapman, Bentley A. Fane, Samuel K. Campos

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Although bacteriophage ϕX174 is easy to propagate and genetically tractable, it is use as a peptide display platform has not been explored. One region within the ϕX174 major spike protein G tolerated 13 of 16 assayed insertions, ranging from 10 to 75 amino acids. The recombinant proteins were functional and incorporated into infectious virions. In the folded protein, the peptides would be icosahedrally displayed within loops that extend from the protein's β-barrel core. The well-honed genetics of ϕX174 allowed permissive insertions to be quickly identified by the cellular phenotypes associated with cloned gene expression. The cloned genes were easily transferred from plasmids to phage genomes via recombination rescue. Direct ELISA validated several recombinant virions for epitope display. Some insertions conferred a temperature-sensitive (ts) protein folding defect, which was suppressed by global suppressors in protein G, located too far away from the insertion to directly alter peptide display.

Original languageEnglish (US)
Pages (from-to)242-248
Number of pages7
JournalVirology
Volume488
DOIs
StatePublished - Jan 15 2016

Keywords

  • Antigen display
  • HPV
  • HPV16
  • L2
  • Microvirus
  • Papillomavirus
  • Peptide display
  • Phage display
  • RG-1
  • ΦX174

ASJC Scopus subject areas

  • Virology

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