Skip to main content
PMC home page
Journal of Virology logoLink to Journal of Virology
. 1974 Feb;13(2):411–418. doi: 10.1128/jvi.13.2.411-418.1974

Structure of the Mouse Mammary Tumor Virus: Polypeptides and Glycoproteins

Yoshio A Teramoto 1, Manuel J Puentes 1, Lawrence J T Young 1, Robert D Cardiff 1
PMCID: PMC355311  PMID: 4359300

Abstract

The polypeptide and glycoprotein compositions of the mouse mammary tumor virus virion from primary monolayer cultures of BALB/cfC3H mouse mammary tumor cells were studied by polyacrylamide gel electrophoresis by using internal and external labeling and Coomassie blue and periodic acid Schiff (PAS) staining. Twelve polypeptides were reproducibly resolved by the combined methods. Five major polypeptides were demonstrable with estimated molecular weights of 52,000, 36,000, 28,000, 14,000, and 10,000. Seven minor polypeptides were also consistently detected and had estimated molecular weights of 70,000, 60,000, 46,000, 38,000, 30,000, 22,000, and 17,000. Carbohydrate was associated with five of these polypeptides as measured by PAS stain or [3H] glucosamine labeling, or both. These glycoproteins had estimated molecular weights of 70,000, 60,000, 52,000, 36,000 and 10,000. The majority of the PAS stain and glucosamine was found in the 52,000 and 36,000 dalton peaks.

Full text

PDF
411

Images in this article

413Image
on p.413
413Image
on p.413
413Image
on p.413
414Image
on p.414
416Image
on p.416

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bentvelzen P. The biology of the mouse mammary tumor virus. Int Rev Exp Pathol. 1972;11:259–297. [PubMed] [Google Scholar]
  2. Blair P. B. Immunology of the mouse mammary tumor virus: comparison of the antigenicity of mammary tumor virus obtained from several strains of mice. Cancer Res. 1970 Mar;30(3):625–631. [PubMed] [Google Scholar]
  3. Blair P. B., Weiss D. W., Pitelka D. R. Immunology of the mouse mammary tumor virus. Correlation of the immunodiffusion precipitate line with type-B virus particles. J Natl Cancer Inst. 1966 Sep;37(3):261–277. doi: 10.1093/jnci/37.3.261. [DOI] [PubMed] [Google Scholar]
  4. Burge B. W., Huang A. S. Comparison of membrane protein glycopeptides of Sindbis virus and vesicular stomatitis virus. J Virol. 1970 Aug;6(2):176–182. doi: 10.1128/jvi.6.2.176-182.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cardiff R. D., Blair P. B., Nakayama P. In vitro cultivation of mouse mammary tumor virus: detection of MTV production by radioisotope labeling and identification by immune precipitation. Proc Natl Acad Sci U S A. 1968 Mar;59(3):895–902. doi: 10.1073/pnas.59.3.895. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cardiff R. D., Blair P. R., DeOme K. B. In vitro cultivation of the mouse mammary tumor virus: replication of MTV in tissue culture. Virology. 1968 Oct;36(2):313–317. doi: 10.1016/0042-6822(68)90152-9. [DOI] [PubMed] [Google Scholar]
  7. Content J., Duesberg P. H. Electrophoretic distribution of the proteins and glycoproteins of influenza virus and Sendai virus. J Virol. 1970 Dec;6(6):707–716. doi: 10.1128/jvi.6.6.707-716.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Duesberg P. H., Martin G. S., Vogt P. K. Glycoprotein components of avian and murine RNA tumor viruses. Virology. 1970 Aug;41(4):631–646. doi: 10.1016/0042-6822(70)90428-9. [DOI] [PubMed] [Google Scholar]
  9. Feldman M. K., Ceriani R. L. A comparative immunologic and electrophoretic analysis of rat and mouse caseins. Comp Biochem Physiol. 1970 Dec 1;37(3):421–427. doi: 10.1016/0010-406x(70)90570-0. [DOI] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. McGrath C. M., Blair P. B. Immunofluorescent localization of mammary tumor virus antigens in mammary tumor cells in culture. Cancer Res. 1970 Jul;30(7):1963–1968. [PubMed] [Google Scholar]
  12. McGrath C. M., Nandi S., Young L. Relationship between organization of mammary tumors and the ability of tumor cells to replicate mammary tumor virus and to recognize growth-inhibitory contact signals in vitro. J Virol. 1972 Feb;9(2):367–376. doi: 10.1128/jvi.9.2.367-376.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. McGrath C. M. Replication of mammary tumor virus in tumor cell cultures: dependence on hormone-induced cellular organization. J Natl Cancer Inst. 1971 Aug;47(2):455–467. [PubMed] [Google Scholar]
  14. Olshevsky U., Becker Y. Surface glycopeptides in the envelope of herpes simplex virions. Virology. 1972 Oct;50(1):277–279. doi: 10.1016/0042-6822(72)90371-6. [DOI] [PubMed] [Google Scholar]
  15. Phillips D. R., Morrison M. The arrangement of proteins in the human erythrocyte membrane. Biochem Biophys Res Commun. 1970 Jul 27;40(2):284–289. doi: 10.1016/0006-291x(70)91007-7. [DOI] [PubMed] [Google Scholar]
  16. Sefton B. M., Wickus G. G., Burge B. W. Enzymatic iodination of Sindbis virus proteins. J Virol. 1973 May;11(5):730–735. doi: 10.1128/jvi.11.5.730-735.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Smith G. H., Wivel N. A. Intracytoplasmic A particles: mouse mammary tumor virus nucleoprotein cores? J Virol. 1973 Apr;11(4):575–584. doi: 10.1128/jvi.11.4.575-584.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Walter G., Mudd J. A. Iodination of vesicular stomatitis virus with lactoperoxidase. Virology. 1973 Apr;52(2):574–577. doi: 10.1016/0042-6822(73)90353-x. [DOI] [PubMed] [Google Scholar]
  19. Witte O. N., Weissman I. L., Kaplan H. S. Structural characteristics of some murine RNA tumor viruses studied by lactoperoxidase iodination. Proc Natl Acad Sci U S A. 1973 Jan;70(1):36–40. doi: 10.1073/pnas.70.1.36. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Journal of Virology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES