Assembly of avian reticuloendotheliosis virus: association of the core precursor polypeptide with the intracellular ribonucleoprotein complex.

A virus-specific ribonucleoprotein complex is present in the cytoplasm of reticuloendotheliosis virus-transformed chicken bone marrow cells. This ribonucleoprotein complex contains viral reverse transcriptase activity and may represent a precursor to the budding virion. The major viral polypeptide associated with the ribonucleoprotein complex was a polypeptide with a molecular weight of 63,000. This protein exhibited a precursor-product relationship with the major reticuloendotheliosis virus structural core protein p29. Core polypeptides were not associated with the intracellular ribonucleoprotein complex. Thus, p29 was incorporated into the virion in the form of its precursor Pr63. The cleavage of Pr63 in the ribonucleoprotein complex was accomplished either during the budding process of shortly after the release of particles from the cell.