Interactions of heterologous DNA with polyomavirus major structural protein, VP1
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10069385
DOI
10.1016/s0014-5793(99)00003-4
PII: S0014-5793(99)00003-4
Knihovny.cz E-resources
- MeSH
- Cell Line MeSH
- Deoxyribonuclease I MeSH
- DNA metabolism MeSH
- Electrophoresis, Agar Gel MeSH
- Capsid genetics metabolism ultrastructure MeSH
- Recombinant Fusion Proteins genetics metabolism ultrastructure MeSH
- Virus Assembly * MeSH
- Spodoptera MeSH
- Capsid Proteins * MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Deoxyribonuclease I MeSH
- DNA MeSH
- Recombinant Fusion Proteins MeSH
- Capsid Proteins * MeSH
- VP1 protein, polyomavirus MeSH Browser
'Empty' polyomavirus pseudocapsids, self-assembled from the major structural protein VP1, bind DNA non-specifically and can deliver it into the nuclei of mammalian cells for expression [Forstová et al. (1995) Hum. Gene Ther. 6, 297-3061. Formation of suitable VP1-DNA complexes appears to be the limiting step in this route of gene delivery. Here, the character of VP1-DNA interactions has been studied in detail. Electron microscopy revealed that VP1 pseudocapsids can create in vitro at least two types of interactions with double-stranded DNA: (i) highly stable complexes, requiring free DNA ends, where the DNA is partially encapsidated; and, (ii) weaker interactions of pseudocapsids with internal parts of the DNA chain.
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