Chemical and Immunological characterization of the major structural protein (p28) of MMC-1, a rhesus monkey endogenous type C virus: homology with the major structural protein of avian reticuloendotheliosis virus.
The major core protein (p28) of MMC-1, an endogenous type C virus of the rhesus monkey (Macaca mulatta), was purified and subjected to structural and immunological analyses. The NH2-terminal amino acid sequence of MMC-1 p28 showed extensive homology to the sequences of the major structural proteins (p30) of known mammalian type C viruses. Similarly, interspecies antigenic determinants shared by all the above viral proteins were detected in MMC-1 p28. Competition radioimmunoassays together with the results of statistical analysis of the primary structure data provided evidence that MMC-1 p28 is not more closely related to primate type C viruses of the Papio genus than to those isolated from rodents, cats, or New World monkeys. MMC-1 p28 was found to be closely related structurally to the p30 protein of the avian reticuloendotheliosis virus (REV-A), a horizontally transmitted type C virus of putative mammalian origin. In addition, MMC-1 p28 and REV-A p30 shared a specific subset of antigenic determinants not present in any of the other avian or mammalian type C viruses studied. These findings suggest that MMC-1 and REV may have a common evolutionary origin.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000956:Antigens, Viral / Q000032:analysis; D003429:Cross Reactions; D000939:Epitopes; D008251:Macaca / Q000382:microbiology*; D008253:Macaca mulatta / Q000382:microbiology*; D001356:Reticuloendotheliosis virus / Q000032:analysis* / Q000276:immunology; D012190:Retroviridae / Q000032:analysis* / Q000276:immunology; D014764:Viral Proteins / Q000032:analysis* / Q000276:immunology
D000596:Amino Acids; D000956:Antigens, Viral; D000939:Epitopes; D014764:Viral Proteins