Characterization of recombinant polioviruses expressing regions of rotavirus VP4, hepatitis B surface antigen, and herpes simplex virus type 2 glycoprotein D

J Virol. 1995 Aug;69(8):5132-7. doi: 10.1128/JVI.69.8.5132-5137.1995.

Abstract

Recombinant polioviruses expressing antigens from rotavirus, herpes simplex virus type 2, and hepatitis B virus were generated. Fusion of the heterologous polypeptides to the amino terminus of the poliovirus polyprotein did not prevent myristylation of VP0, suggesting a novel mechanism of myristylation for these recombinant viruses. The effects of the parental genetic background, different foreign sequences, and different insert sizes on growth characteristics were compared. Both the size and the nature of the heterologous sequence appeared to be factors influencing the growth and stability of recombinant polioviruses. All of the recombinants showed a temperature-sensitive phenotype, regardless of the genetic background (attenuated or wild type) from which they were derived. Preliminary studies with transgenic mice carrying the poliovirus receptor gene are discussed.

MeSH terms

  • Animals
  • Antibodies, Viral / immunology
  • Capsid / chemistry
  • Capsid / genetics*
  • Capsid / metabolism
  • Capsid Proteins*
  • Chlorocebus aethiops
  • Genetic Vectors
  • HeLa Cells
  • Hepatitis B Surface Antigens / genetics*
  • Hepatitis B Surface Antigens / metabolism
  • Hot Temperature
  • Humans
  • Mice
  • Mice, Transgenic
  • Myristic Acid
  • Myristic Acids / metabolism
  • Peptide Fragments / immunology
  • Poliovirus / genetics*
  • Poliovirus / metabolism
  • Poliovirus / physiology
  • Recombination, Genetic
  • Vero Cells
  • Viral Envelope Proteins / genetics*
  • Viral Envelope Proteins / metabolism
  • Virus Replication

Substances

  • Antibodies, Viral
  • Capsid Proteins
  • Hepatitis B Surface Antigens
  • Myristic Acids
  • Peptide Fragments
  • VP4 protein, Rotavirus
  • Viral Envelope Proteins
  • glycoprotein D-herpes simplex virus type 2
  • Myristic Acid