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New insights into the role of RNase L in innate immunity Chakrabarti A; Jha BK; Silverman RHJ Interferon Cytokine Res 2011[Jan]; 31 (1): 49-57The interferon (IFN)-inducible 2'-5'-oligoadenylate synthetase (OAS)/RNase L pathway blocks infections by some types of viruses through cleavage of viral and cellular single-stranded RNA. Viruses induce type I IFNs that initiate signaling to the OAS genes. OAS proteins are pathogen recognition receptors for the viral pathogen-associated molecular pattern, double-stranded RNA. Double-stranded RNA activates OAS to produce p(x)5'A(2'p5'A)(n); x = 1-3; n > 2 (2-5A) from ATP. Upon binding 2-5A, RNase L is converted from an inactive monomer to a potently active dimeric endoribonuclease for single-stranded RNA. RNase L contains, from N- to C-terminus, a series of 9 ankyrin repeats, a linker, several protein kinase-like motifs, and a ribonuclease domain homologous to Ire1 (involved in the unfolded protein response). In the past few years, it has become increasingly apparent that RNase L and OAS contribute to innate immunity in many ways. For example, small RNA cleavage products produced by RNase L during viral infections can signal to the retinoic acid-inducible-I like receptors to amplify and perpetuate signaling to the IFN-beta gene. In addition, RNase L is now implicated in protecting the central nervous system against viral-induced demyelination. A role in tumor suppression was inferred by mapping of the RNase L gene to the hereditary prostate cancer 1 (HPC1) gene, which in turn led to discovery of the xenotropic murine leukemia-related virus. A broader role in innate immunity is suggested by involvement of RNase L in cytokine induction and endosomal pathways that suppress bacterial infections. These newly described findings about RNase L could eventually provide the basis for developing broad-spectrum antimicrobial drugs.|*Immunity, Innate[MESH]|2',5'-Oligoadenylate Synthetase/genetics/metabolism[MESH]|Animals[MESH]|Antigens, Surface/metabolism[MESH]|Demyelinating Diseases/prevention & control[MESH]|ELAV Proteins[MESH]|ELAV-Like Protein 1[MESH]|Endoribonucleases/genetics/*metabolism[MESH]|Gene Expression Regulation[MESH]|Host-Pathogen Interactions[MESH]|Humans[MESH]|Interferons/genetics/metabolism[MESH]|Neoplasms/immunology/metabolism[MESH]|Protein Interaction Domains and Motifs[MESH]|RNA, Double-Stranded/metabolism[MESH]|RNA, Messenger/metabolism[MESH]|RNA, Viral/metabolism[MESH]|RNA-Binding Proteins/metabolism[MESH]|Sequence Homology, Amino Acid[MESH]|Virus Diseases/immunology/metabolism[MESH] |
