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VIRAL ASSEMBLY

The TRiCky business of reovirus assembly

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The TRiC chaperonin has been identified as a crucial player in the assembly of reovirus capsids by folding the σ3 outer-capsid protein into its native conformation. These findings provide a functional understanding of TRiC in virus replication and a rationale for the development of TRiC inhibitors as broad-spectrum anti-viral agents.

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Fig. 1: Reovirus σ3 protein requires the TRiC chaperonin for folding into native conformers.

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Authors and Affiliations

  1. Department of Veterinary Microbiology and Preventive Medicine, College of Veterinary Medicine, Iowa State University, Ames, IA, USA

    Cathy L. Miller

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  1. Cathy L. Miller
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Correspondence to Cathy L. Miller.

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The author declares no competing interests.

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Miller, C.L. The TRiCky business of reovirus assembly. Nat Microbiol 3, 400–401 (2018). https://doi.org/10.1038/s41564-018-0137-3

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