Structure of the Mouse Mammary Tumor Virus: Characterization of Bald Particles

Author:

Cardiff R. D.1,Puentes M. J.1,Teramoto Y. A.1,Lund J. K.1

Affiliation:

1. Department of Pathology, School of Medicine, University of California, Davis, California 95616

Abstract

The polypeptide, antigenic, and morphological structure of the mouse mammary tumor virus was studied following protease digestion of intact virions. Intact, untreated virions (ρ = 1.17 g/ml) had characteristic envelope spikes, five major polypeptides, and were precipitated by antisera against gp52. Two of the major polypeptides, with molecular weights of 52,000 (gp52) and 36,000 (gp36), had carbohydrate moieties. Protease treatment resulted in spikeless, “bald” particles (ρ = 1.14 g/ml), which had altered surface antigenicity and which contained neither gp52 nor gp36. These data indicated that gp52 and gp36 were on the viral envelope. Bald particles retained a 28,000 dalton polypeptide (p28) which was proposed as the major internal polypeptide.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

Reference27 articles.

1. Immunology of the mouse mammary tumor virus: comparison of the antigenicity of mammary tumor virus obtained from several strains of mice;Blair P. B.;Cancer Res.,1970

2. Localization of RNA tumor virus polypeptides. I. Isolation of further virus substructures;Bolognesi D. P.;Virology,1973

3. Quantitation of mouse mammary tumor virus (MTV) virions by radioimmunoassay;Cardiff R. D.;J. Immunol.,1973

4. In vitro cultivation of the mouse mammary tumor virus: replication of MTV in tissue cultures;Cardiff R. D.;Virology,1968

5. In vitro cultivation of the mouse mammary tumor virus: correlation of infectivity and morphology with radioisotope studies;Cardiff R D;Int. J. Cancer,1970

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