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Mol Cell. 2015 May 7;58(3):541-548. doi: 10.1016/j.molcel.2015.03.014. Epub 2015 Apr 16.

ATP-dependent effector-like functions of RIG-I-like receptors.

Author information

Program in Cellular and Molecular Medicine, Children's Hospital Boston, MA 02115, USA.
State Key Laboratory of Medicinal Chemical Biology, College of Life Sciences Nankai University, Tianjin 300071, China.
Laboratory of Virology and Infectious Disease, Center for the Study of Hepatitis C The Rockefeller University, New York, New York 10065, USA.
Department of Biological Chemistry and Molecular Pharmacology Harvard Medical School, Boston, MA 02115, USA.
Institut für Molekulare Medizin, Universitätsklinikum Bonn, 53127 Bonn, Germany.
Contributed equally


The vertebrate antiviral innate immune system is often considered to consist of two distinct groups of proteins: pattern recognition receptors (PRRs) that detect viral infection and induce the interferon (IFN) signaling, and effectors that directly act against viral replication. Accordingly, previous studies on PRRs, such as RIG-I and MDA5, have primarily focused on their functions in viral double-stranded RNA (dsRNA) detection and consequent antiviral signaling. We report here that both RIG-I and MDA5 efficiently displace viral proteins pre-bound to dsRNA in a manner dependent on their ATP hydrolysis, and that this activity assists a dsRNA-dependent antiviral effector protein, PKR, and allows RIG-I to promote MDA5 signaling. Furthermore, truncated RIG-I/MDA5 lacking the signaling domain, and hence the IFN stimulatory activity, displaces viral proteins and suppresses replication of certain viruses in an ATP-dependent manner. Thus, this study reveals novel "effector-like" functions of RIG-I and MDA5 that challenge the conventional view of PRRs.

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