Monoclonal antibodies specific for the virion polypeptide, p27, of avian retroviruses

• Published in: Hybridoma Vol. 3; no. 1; p. 25
• Main Authors: Parsons, S J, Wilson, L D, Ely, C M, Parsons, J T, Benjamin, D C
• Format: Journal Article
• Language: English
• Published: United States 1984
• Subjects: Alpharetrovirus - immunology; Animals; Antibodies, Monoclonal - immunology; Antibodies, Viral - immunology; Antibody Specificity; Antigens, Viral - immunology; Binding, Competitive; Cell Transformation, Viral; Chick Embryo; Epitopes - immunology; Hybridomas - immunology; Mice; Oncogene Protein pp60(v-src); Retroviridae Proteins; Viral Proteins - immunology
• ISSN: 0272-457X
• DOI: 10.1089/hyb.1984.3.25

The major component of the core structure of avian sarcoma leukosis viruses is a 27 kD molecular weight polypeptide, p27. Spleen cells from mice immunized with the Schmidt-Ruppin strain of Rous sarcoma virus (RSV) were fused with mouse myeloma cells (SP2/0), and hybridoma cell lines producing monoclonal antibodies to p27 were isolated. The monoclonal antibodies were all of the IgG1 subclass with kappa light chains. These antibodies immunoprecipitated p27 and its precursor proteins from extracts of RSV-transformed cells. Reciprocal competitive binding experiments defined five nonoverlapping antigenic determinants within p27. The monoclonal antibodies also immunoprecipitated the transforming protein, p110gag-myc, from avian myelocytomatosis virus transformed cells. Their usefulness in studies of virion maturation and viral oncogenesis is discussed.