Abstract
The polypeptides of reticuloendotheliosis virus (REV) were separated by gel filtration in the presence of guanidine hydrochloride. The eight peaks obtained by gel filtration were then analyzed by polyacrylamide gel electrophoresis and four appeared to contain single polypeptides. The material identified as p29 was used to prepare 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 a 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.
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
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