INTRODUCTION: SIGNIFICANCE OF THE PAPER

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Ribonuclease L is part of the body’s innate immune defense, to wit, the antiviral state of the cell. A cell is highly resistant to viral attacks and is also ready to undergo apoptosis upon successful viral infection.  The cell’s last stand against a virus before it attempts apoptosis is the deterioration of all RNA within the cell that usually occurs with cessation of translation activity caused by Protein kinase R.

     In the infected cell, Rnase L and MDA5 (melanoma differentiation-associated protein 5) produce interferon beta (INF-β), a type I interferon responsible for antiviral activity. The relationship between RNAse L and MDA5 in the production of INFs has been confirmed with siRNA tests silencing the expression of either molecule and noting a marked decline in INF production. MDA5, an RNA helicase, is known to be activated by long dsRNA transcribed from the viral genome. In a cell with RNAse L, MDA5 activity may be further enhanced. When active, RNAse L cleaves and identifies viral RNA and feeds it into MDA5 activation sites, enhancing the production of INF-β. The RNA fragments produced by RNAse L have double stranded regions, as well as specific markers,   that allow them to be identified by the RNAse L and MDA5. Some studies have suggested that high levels of RNAse L may actually inhibit INF-β production, but a clear linkage still exists between RNAse L activity and INF-β production.

Naming

Name of Protein	Short name
2'-5' oligoadenylate synthetase-dependent ribonuclease	2-5A-dependent ribonuclease  2-5A-dependent RNase

            

Alternative name(s)	Short name
Ribonuclease 4 Ribonuclease L	RNase L