Neurovirulence of polytropic murine retrovirus is influenced by two separate regions on opposite sides of the envelope protein receptor binding domain

J Virol. 2008 Sep;82(17):8906-10. doi: 10.1128/JVI.02134-07. Epub 2008 Jun 25.

Abstract

Changes in the envelope proteins of retroviruses can alter the ability of these viruses to infect the central nervous system (CNS) and induce neurological disease. In the present study, nine envelope residues were found to influence neurovirulence of the Friend murine polytropic retrovirus Fr98. When projected on a three-dimensional model, these residues were clustered in two spatially separated groups, one in variable region B of the receptor binding site and the other on the opposite side of the envelope. Further studies indicated a role for these residues in virus replication in the CNS, although the residues did not affect viral entry.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Animals, Newborn
  • Leukemia Virus, Murine / isolation & purification
  • Leukemia Virus, Murine / pathogenicity*
  • Leukemia, Experimental / pathology*
  • Mice
  • Mice, Inbred Strains
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Receptors, Virus / metabolism
  • Retroviridae Infections / pathology*
  • Sequence Homology, Amino Acid
  • Tumor Virus Infections / pathology*
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / isolation & purification
  • Viral Envelope Proteins / metabolism*
  • Virulence / genetics

Substances

  • Receptors, Virus
  • Viral Envelope Proteins