Amino-terminal amino acid sequence of the major structural polypeptides of avian retroviruses: Sequence homology between reticuloendotheliosis virus p30 and p30s of mammalian retroviruses

Academic Article

Abstract

  • The major structural polypeptides, p30 of reticuloendotheliosis virus (REV) (strain T) and p27 of avian sarcoma virus B77, have been compared with regard to amino acid composition, NH2-terminal amino acid sequence, and immunological crossreaction. The amino acid composition of the two polypeptides is distinct, and a comparison of the first 30 NH2-terminal amino acids of REV p30 with that of the first 25 of B77 p27 yields only three homologous residues. In competition radioimmunoassays the polypeptides show no crossreactivity. A comparison of the amino acid composition and NH2-terminal amino acid sequence of REV p30 with those reported for several mammalian retrovirus p30s shows remarkable similarities. Both REV and mammalian p30s contain a large number of polar residues in their amino acid composition and show approximately 40% homology in the first 30 NH2-terminal amino acids. No crossreactivity could be observed, however, in competition radioimmunoassays between Rauscher murine leukemia virus p30 and that of REV. The observations reported here suggest a close evolutionary relationship between REV and the mammalian retroviruses.
  • Authors

    Digital Object Identifier (doi)

    Author List

  • Hunter E; Bhown AS; Bennett JC
  • Start Page

  • 2708
  • End Page

  • 2712
  • Volume

  • 75
  • Issue

  • 6