Large T antigens of many polyomaviruses are able to form complexes with the retinoblastoma protein

J Virol. 1990 Mar;64(3):1353-6. doi: 10.1128/JVI.64.3.1353-1356.1990.

Abstract

Stable protein complexes between the large T antigens of mouse, monkey, baboon, or human polyomaviruses and the retinoblastoma protein were detected by an in vitro coimmunoprecipitation assay. All of the large T antigens tested were able to bind to both human and mouse retinoblastoma polypeptides, showing that these interactions have been conserved during evolution.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antigens, Polyomavirus Transforming* / analysis
  • Antigens, Polyomavirus Transforming* / genetics
  • Haplorhini
  • Humans
  • Molecular Sequence Data
  • Nuclear Proteins*
  • Papio
  • Phosphoproteins* / analysis
  • Phosphoproteins* / metabolism
  • Polyomavirus / genetics
  • Polyomavirus / immunology*
  • Protein Binding
  • Retinoblastoma Protein
  • Sequence Homology, Nucleic Acid

Substances

  • Antigens, Polyomavirus Transforming
  • Nuclear Proteins
  • Phosphoproteins
  • Retinoblastoma Protein