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. 1974 Nov;14(5):1293–1303. doi: 10.1128/jvi.14.5.1293-1303.1974

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

R D Cardiff 1, M J Puentes 1, Y A Teramoto 1, J K Lund 1
PMCID: PMC355648  PMID: 4372399

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.

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Selected References

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

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