Murine mammary tumor virus structural protein interactions: formation of oligomeric complexes with cleavable cross-linking agents

  • Racevskis J
  • Sarkar N
24Citations
Citations of this article
5Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

Murine mammary tumor virus protein interactions in the intact virion structure were studied with the use of the cleavable cross-linking reagents dithiobis(succinimidyl propionate) and methyl 4-mercaptobutyrimidate hydrochloride. Cross-linked oligomeric complexes of murine mammary tumor virus proteins were analyzed by two-dimensional gel electrophoresis. Among the complexes most consistently formed were a heterodimer of the two glycoproteins gp36 and gp52, the homodimer of gp36, and the homotrimer of gp52. A very prominent oligomer formed at higher concentrations of dithiobis(succinimidyl propionate) was a complex of about 230,000 molecular weight, made up of three molecules each of gp36 and gp52. A number of lines of evidence, including electron microscopic analysis, suggest that the 230,000-molecular-weight complex actually represents the murine mammary tumor virus spike structure. Of the murine mammary tumor virus core proteins, p14 forms homooligomers most readily. Upon cross-linking with methyl 4-mercaptobutyrimidate hydrochloride a small amount of what seems to be a heterodimer made up of the N-terminal gag protein p10 and the hydrophobic membrane glycoprotein gp36 can be observed.

Cite

CITATION STYLE

APA

Racevskis, J., & Sarkar, N. H. (1980). Murine mammary tumor virus structural protein interactions: formation of oligomeric complexes with cleavable cross-linking agents. Journal of Virology, 35(3), 937–948. https://doi.org/10.1128/jvi.35.3.937-948.1980

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free