Antiviral transgenic plants, vectors, cells and methods
US5861300A · kind A · utility
Assignee
Inventors
Key dates
| Filing date | May 8, 1995 |
| Grant date | Jan 19, 1999 |
| Priority date | — |
| Expiry date | May 8, 2015 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC12N15/8283
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
Isolated 2-5A-dependent RNases, an interferon-induced enzyme which is activated by 5'-phosphorylated, 2',5'-linked oligoadenylates (2-5A) and implicated in both the molecular mechanisms of interferon action and in the fundamental control of RNA stability in mammalian cells, and encoding sequences therefor are disclosed. The expression cloning and analysis of murine and human 2-5A-dependent RNases is also disclosed. Recombinant human 2-5A-dependent RNase produced in vitro bound an activating affinity matrix, 2-5A-cellulose, resulting in ribonuclease activity. The 2-5A binding properties of the recombinant and naturally occurring forms of 2-5A-dependent RNase are basically identical. Interferon induction of 2-5A-dependent RNase expression is demonstrated by measuring the mRNA levels in cells treated with interferon and cycloheximide. Analysis of aligned murine and human 2-5A-dependent RNase sequences revealed several features, including similarity to RNase E which is implicated in the control of mRNA stability in E. coli. A duplicated phosphate-binding loop motif is determined by deletion analysis and site-directed mutagenesis to function in the binding of 2-5A. In addition, recombin…
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