title: Inhibition of the OAS/RNase L pathway by viruses.
abstract: The OAS/RNase L system was one of the first characterized interferon effector pathways. It relies on the synthesis, by oligoadenylate synthetases (OAS), of short oligonucleotides that act as second messengers to activate the latent cellular RNase L. Viruses have developed diverse strategies to escape its antiviral effects. This underscores the importance of the OAS/RNase L pathway in antiviral defenses. Viral proteins such as the NS1 protein of Influenza virus A act upstream of the pathway while other viral proteins such as Theiler's virus L* protein act downstream. The diversity of escape strategies used by viruses likely stems from their relative susceptibility to OAS/RNase L and other antiviral pathways, which may depend on their host and cellular tropism.
authors.affiliation: Université catholique de Louvain, de Duve Institute, Brussels, Belgium.
authors.forename: Melissa
authors.initials: M
authors.lastname: Drappier
authors.affiliation: Université catholique de Louvain, de Duve Institute, Brussels, Belgium. Electronic address: thomas.michiels@uclouvain.be.
authors.forename: Thomas
authors.initials: T
authors.lastname: Michiels
mesh_terms: D015088:2',5'-Oligoadenylate Synthetase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D001483:Base Sequence; D004722:Endoribonucleases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D006801:Humans; D012328:RNA Viruses / Q000235:genetics / Q000378:metabolism*; D017361:Viral Nonstructural Proteins / Q000378:metabolism; D014764:Viral Proteins / Q000037:antagonists & inhibitors* / Q000378:metabolism; D014777:Virus Diseases / Q000201:enzymology*
chemical_list: C085820:INS1 protein, influenza virus; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; D015088:2',5'-Oligoadenylate Synthetase; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease