Affiliation:
1. Department of Pathology, University of Colorado Medical Center, Denver, Colorado 80262
2. Department of Microbiology, Rush Medical School, Chicago, Illinois 60612
Abstract
Genetic analyses have defined a single gene (
src
) as that portion of the avian sarcoma virus (ASV) genome which encodes the protein directly responsible for ASV-induced neoplastic transformation. We have recently identified the polypeptide product of the
src
gene of the Schmidt-Ruppin (SR) strain of ASV, a 60,000-dalton phosphoprotein designated pp60
src
, and have further determined that pp60
src
acts as a protein kinase. Essential to the identification and characterization of the pp60
src
protein of SR-ASV was the use of serum (TBR serum) from rabbits bearing SR-ASV-induced tumors. TBR serum was, however, strain specific, recognizing pp60
src
from SR-ASV-transformed cells only. We report here that sera from marmosets bearing tumors induced by the Bryan or SR strains of ASV (TBM sera) contain antibody which precipitates the transforming gene product from cells transformed by the SR, Bryan, Prague, or Bratislava strains of ASV. In contrast, rabbits bearing tumors induced by either the Bratislava or Bryan strains of ASV, or hamsters with SR-ASV-induced tumors did not produce antibody to pp60
src
from any strain of ASV. The 60,000-dalton polypeptides immunoprecipitated with TBM serum from cells transformed by each of the above virus strains are phosphoproteins. One-dimensional peptide mapping by limited proteolysis revealed that the pp60
src
proteins are structurally very similar, but not identical. Furthermore, all of the viral pp60
src
proteins have an associated phosphotransferase activity. In addition to detecting the viral
src
proteins, TBM serum was able to immunoprecipitate an antigenically related protein from normal uninfected avian cells.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Cited by
44 articles.
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