Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1977 Aug;74(8):3446–3450. doi: 10.1073/pnas.74.8.3446

Murine leukemia virus morphogenesis: cleavage of P70 in vitro can be accompanied by a shift from a concentrically coiled internal strand ("immature") to a collapsed ("mature") form of the virus core.

Y Yoshinaka, R B Luftig
PMCID: PMC431601  PMID: 410020

Abstract

Disruption of Rauscher leukemia virus (RLV) with low levels of Nonidet P-40 yielded "immature" cores. These cores have a diameter of about 920 A, as opposed to the 1300-A diameter of RLV, possess knob-like protuberances, and contain a concentrically coiled internal strand apposed to the core shell. The two major polypeptide components of immature cores are (i) p30, the 30,000-dalton group-specific antigen, and (ii) a polypeptide that has the size and antigenic characteristics of P70, the 70,000-dalton precursor protein of the group-specific antigens of murine leukemia virus. Disruption of RLV at high ratios of Nonidet P-40 to virus yielded "mature" cores. These cores have an average diameter of 850 A, a smooth proteinaceous perimeter, and a collapsed internal strand, and they contain predominantly p30. Treatment of RLV with low levels of Nonidet P-40 for 16 hr at 22 degrees yielded cores that showed (I) a 70% decrease in the number of immature forms and concomitant increase in the number of mature forms, (II) a 60-90% decrease of P70, and (iii) a 30% increase in a 40,000- to 42,000-dalton protein. These results suggest that maturation of RLV cores is accomplished by cleavage of P70.

Full text

PDF
3446

Images in this article

3447Image
on p.3447
3447Image
on p.3447
3448Image
on p.3448
3448Image
on p.3448
3449Image
on p.3449
3449Image
on p.3449
3449Image
on p.3449

Selected References

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

  1. August J. T., Bolognesi D. P., Fleissner E., Gilden R. V., Nowinski R. C. A proposed nomenclature for the virion proteins of oncogenic RNA viruses. Virology. 1974 Aug;60(2):595–600. doi: 10.1016/0042-6822(74)90356-0. [DOI] [PubMed] [Google Scholar]
  2. Barbacid M., Stephenson J. R., Aaronson S. A. gag Gene of mammalian type-C RNA tumour viruses. Nature. 1976 Aug 12;262(5569):554–559. doi: 10.1038/262554a0. [DOI] [PubMed] [Google Scholar]
  3. Bolognesi D. P., Luftig R., Shaper J. H. Localization of RNA tumor virus polypeptides. I. Isolation of further virus substructures. Virology. 1973 Dec;56(2):549–564. doi: 10.1016/0042-6822(73)90057-3. [DOI] [PubMed] [Google Scholar]
  4. Eisenman R., Vogt V. M., Diggelmann H. Synthesis of avian RNA tumor virus structural proteins. Cold Spring Harb Symp Quant Biol. 1975;39(Pt 2):1067–1075. doi: 10.1101/sqb.1974.039.01.122. [DOI] [PubMed] [Google Scholar]
  5. Horzinek M., Mussgay M. Studies on the nucleocapsid structure of a group A arbovirus. J Virol. 1969 Oct;4(4):514–520. doi: 10.1128/jvi.4.4.514-520.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Ikeda H., Hardy W., Jr, Tress E., Fleissner E. Chromatographic separation and antigenic analysis of proteins of the oncornaviruses. V. Identification of a new murine viral protein, p15(E). J Virol. 1975 Jul;16(1):53–61. doi: 10.1128/jvi.16.1.53-61.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Jamjoom G. A., Naso R. B., Arlinghaus R. B. Selective decrease in the rate of cleavage of an intracellular precursor to Rauscher leukemia virus p30 by treatment of infected cells with actinomycin D. J Virol. 1976 Sep;19(3):1054–1072. doi: 10.1128/jvi.19.3.1054-1072.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Luftig R. B., Kilham S. S. An electron microscope study of Rauscher leukemia virus. Virology. 1971 Nov;46(2):277–297. doi: 10.1016/0042-6822(71)90030-4. [DOI] [PubMed] [Google Scholar]
  11. Luftig R. B., McMillan P. N., Bolognesi D. P. An ultrastructural study of C-type virion assembly in mouse cells. Cancer Res. 1974 Dec;34(12):3303–3310. [PubMed] [Google Scholar]
  12. Seifert E., Claviez M., Frank H., Hunsmann G., Schwarz H., Schäfer W. XII. Produktion grösserer Mengen von Friend-Virus durch eine permanente Zell-Suspensions-Kultur (Eveline-Suspensions-Zellen) Z Naturforsch C. 1975 Sep-Oct;30(5):698–700. [PubMed] [Google Scholar]
  13. Shapiro S. Z., Strand M., August J. T. High molecular weight precursor polypeptides to structural proteins of Rauscher murine leukemia virus. J Mol Biol. 1976 Nov 15;107(4):459–477. doi: 10.1016/s0022-2836(76)80078-2. [DOI] [PubMed] [Google Scholar]
  14. de Harven E. Remarks on the ultrastructure of type A, B, and C virus particles. Adv Virus Res. 1974;19:221–264. doi: 10.1016/s0065-3527(08)60661-2. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES