Chimeric papillomavirus-like particles

Virology. 1997 Jul 21;234(1):93-111. doi: 10.1006/viro.1997.8591.

Abstract

We have constructed chimeric papillomavirus-like particles (CVLPs) by replacing the 34-carboxy-terminal amino acids of the HPV 16 L1 protein with various parts of the HPV 16 E7 protein. Chimeric proteins were expressed by recombinant baculoviruses and analyzed by electron microscopy for their ability to assemble into virus capsids. We were able to produce CVLPs in high efficiencies with inserts of up to 60 amino acids. CVLPs are able to induce a neutralizing antibody response, assayed by inhibition of hemagglutination of mouse erythrocytes. CVLPs are interacting with the putative receptor for papillomaviruses as they were shown to hemagglutinate mouse red blood cells and bind to and penetrate cells in vitro. As CVLPs follow a similar intracellular pathway as observed earlier for BPV VLPs, we speculate that CVLPs can be used to deliver peptides into mammalian cells in vitro and in vivo, possibly reaching the pathway for MHC class I presentation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies, Viral / biosynthesis
  • Capsid Proteins*
  • Cell Line
  • Chlorocebus aethiops
  • Humans
  • Immunization
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Oncogene Proteins, Viral / genetics
  • Oncogene Proteins, Viral / metabolism
  • Papillomaviridae / genetics*
  • Papillomaviridae / immunology
  • Papillomaviridae / metabolism
  • Papillomaviridae / physiology
  • Papillomavirus E7 Proteins
  • Recombination, Genetic*
  • Spodoptera / cytology
  • Virion
  • Virus Assembly

Substances

  • Antibodies, Viral
  • Capsid Proteins
  • Oncogene Proteins, Viral
  • Papillomavirus E7 Proteins
  • oncogene protein E7, Human papillomavirus type 16
  • L1 protein, Human papillomavirus type 16