title: Amino-terminal amino acid sequence of the major structural polypeptides of avian retroviruses: sequence homology between reticuloendotheliosis virus p30 and p30s of mammalian retroviruses.
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 crossreactions. 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 for 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.
mesh_terms: D000595:Amino Acid Sequence; D000956:Antigens, Viral / Q000032:analysis; D001358:Avian Sarcoma Viruses / Q000276:immunology; D009052:Leukemia Virus, Murine / Q000276:immunology; D011925:Rauscher Virus / Q000276:immunology; D001356:Reticuloendotheliosis virus / Q000276:immunology; D012190:Retroviridae / Q000276:immunology; D014764:Viral Proteins / Q000276:immunology
chemical_list: D000956:Antigens, Viral; D014764:Viral Proteins