Immunology

Prions May Do Good, Too

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Science  02 Sep 2011:
Vol. 333, Issue 6047, pp. 1201
DOI: 10.1126/science.333.6047.1201-c

Prions are the causative agent in fatal neurological diseases affecting humans and animals. Prions are a native protein conformation's Mr. Hyde: They adopt a particular conformation that induces self-perpetuating protein aggregation, which can lead to devastating effects. Recent evidence suggests that not all prions are bad, however, and now Hou et al. show that effective antiviral immunity may depend on the formation of prion-like aggregates of the protein MAVS. MAVS functions downstream of RIG-I, an RNA helicase important for detecting viruses. RIG-I induced formation of MAVS prion-like fibrils in response to viral infection. These fibrils were resistant to detergent and protease and were able to “infect” endogenous MAVS proteins—that is, convert native MAVS into fibrils. These characteristics are all hallmarks of prions, which suggest that organisms can also use prions to their own advantage.

Cell 146, 448 (2011).

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