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The noncanonical Gag domains p8 and n are critical for assembly and release of mouse mammary tumor virus
A. Zábranský, P. Hoboth, R. Hadravová, J. Stokrová, M. Sakalian, I. Pichová,
Language English Country United States
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
Free Medical Journals
from 1967 to 6 months ago
Freely Accessible Science Journals
from 1967 to 6 months ago
PubMed Central
from 1967 to 6 months ago
Europe PubMed Central
from 1967 to 6 months ago
Open Access Digital Library
from 1967-02-01
Open Access Digital Library
from 1967-02-01
PubMed
20739518
DOI
10.1128/jvi.00652-10
Knihovny.cz E-resources
- MeSH
- Gene Products, gag physiology MeSH
- Mice MeSH
- Virus Assembly MeSH
- Protein Structure, Tertiary MeSH
- Capsid Proteins MeSH
- Mammary Tumor Virus, Mouse physiology MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
The mouse mammary tumor virus (MMTV) Gag contains the unique domains pp21, p3, p8, and n. We investigated the contribution of these domains to particle assembly and found that the region spanning the p8 and n domains is critical for shape determination and assembly. Deletion of pp21 and p3 reduced the number of released particles, but deletion of the n domain resulted in frequent formation of aberrant particles, while deletion of p8 severely impaired assembly. Further investigation of p8 revealed that both the basic and the proline-rich motifs within p8 contribute to MMTV assembly.
References provided by Crossref.org
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