La voie OAS/RNase L et son inhibition par les virus
(2014) Virologie — Vol. 18, n° 5, p. 1026-1036 (2014)
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- Authors
Michiels, Thomas 
- Abstract
- RNase L is a well-known effector of the type I interferon pathway. This review focuses on the recent developments of RNase L activation and on the antagonism of the OAS-RNase L pathway by viral proteins. Recent structural data show that two 2'-5' oligoadenylate molecules can bridge ankyrin domains of two RNase L subunits bound in opposite orientations. The binding of nucleotides to the pseudokinase domain further strengthens the dimer and imparts an active conformation to the ribonuclease. The OAS/RNase L pathway is active against many viruses and viruses evolved in several ways to escape this pathway. Influenza virus A acts upstream of this pathway by hiding double stranded RNA through its NS1 protein. In this way, it also inhibits the PKR and TLR-3 activation by double stranded RNA. Theiler's virus acts downstream of the OAS/RNase L pathway, through the direct interaction between protein L*and RNase L. By acting on the effector enzyme, Theiler's virus ensures a strong RNase L inhibition, which seems to be particularly useful for the infection of macrophages. In conclusion, viruses have developed distinct strategies to escape RNase L activity, that are likely dependent on their tropism. The fact that viral proteins have evolved to specifically antagonize RNase L outlines the importance of this particular IFN effector in cells infected by those viruses.
Citations
Drappier, M., Michiels, T., & Sorgeloos, F. (2014). La voie OAS/RNase L et son inhibition par les virus. Virologie, 18(5), 1026-1036. https://hdl.handle.net/2078.5/48477 (Original work published 2014)