Abstract
The polypeptides of reticuloendotheliosis virus (REV) were separated by gel filtration in the presence of guanidine hydrochloride. The 8 peaks obtained by gel filtration were then analyzed by polyacrylamide gel electrophoresis and 4 appeared to contain single polypeptides. The material identified as p29 was used to prepare [rabbit] antiserum. This protein constitutes the major internal non-glycosylated polypeptide in the virion. Double immunodiffusion indicated that the antiserum was specific for p29. Using this antiserum, cross-reactivity was demonstrated between REV, chick syncytial virus, duck infectious anemia virus and spleen necrosis virus. Antiserum to p29 failed to cross-react with Rous sarcoma virus. This indicates that p29 is group-specific antigen shared by the viruses of the REV complex. A microcomplement fixation test was developed with this antiserum that will be useful in the quantitation of REV and the identification of other members of this newly defined group.