Human Breast Carcinoma Antigen is Immunologically Related to the Polypeptide of the Group-Specific Glycoprotein of Mouse Mammary Tumor Virus

• Published in: Proceedings of the National Academy of Sciences - PNAS 1979-05, Vol.76 (5), p.2460-2464
• Main Authors: Ohno, T., Mesa-Tejada, R., Keydar, I., Ramanarayanan, M., Bausch, J., Spiegelman, S.
• Format: Article
• Language: English
• Subjects: Animals; Antibodies; Antigens; Antigens, Neoplasm - analysis; Antigens, Viral - analysis; Apoproteins - immunology; Breast cancer; Breast Neoplasms - immunology; Breasts; Carcinoma - immunology; Carcinoma in Situ - immunology; Carcinoma, Intraductal, Noninfiltrating - immunology; Cross Reactions; Epitopes; Female; Gels; Glycoproteins; Glycoproteins - immunology; Humans; Immunology; Mammary Tumor Virus, Mouse - immunology; Mice; Sugars; Viral Proteins - immunology; Viruses
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.76.5.2460

We have shown [Mesa-Tejada, R., Keydar, I., Ramanarayanan, M., Ohno, T., Fenoglio, C. & Spiegelman, S. (1978) Proc. Natl. Acad. Sci. USA 75, 1529-1533] that an antigen immunologically related to gp52, a 52,000-dalton glycoprotein of the mouse mammary tumor virus, can be identified in sections of human breast cancer by means of an indirect immunoperoxidase technique. The specificity of the reaction was established by absorption experiments which revealed that only purified gp52, or material containing it, served to eliminate the IgG molecules responsible for the immunohistochemical reaction in the human breast tumors. We show here that the cross-reactivity between the human and murine tumor antigens is due to the polypeptide rather than the polysaccharide components of gp52. Sugar-free gp52 prepared by deglycosylation with a mixture of glycosidases was as fully effective as the intact gp52 in removing from anti-MMTV the IgG responsible for the reaction with the human tumor antigen. In contrast, the isolated polysaccharide of gp52 was unable to exert blocking activity.