Lipids Cooperate with the Reovirus Membrane Penetration Peptide to Facilitate Particle Uncoating
- ↵1 To whom correspondence should be addressed: Dept. of Biology, Indiana University, Simon Hall MSB1, 212 South Hawthorne Drive, Bloomington, IN 47405-7003. Tel.: 812-856-2449; Fax: 812-856-5710; E-mail: pdanthi{at}indiana.edu.
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Edited by Charles Samuel
Abstract
Virus-host interactions play a role in many stages of the viral lifecycle, including entry. Reovirus, a model system for studying the entry mechanisms of nonenveloped viruses, undergoes a series of regulated structural transitions that culminate in delivery of the viral genetic material. Lipids can trigger one of these conformational changes, infectious subviral particle (ISVP)-to-ISVP* conversion. ISVP* formation releases two virally encoded peptides, myristoylated μ1N (myr-μ1N) and Φ. Among these, myr-μ1N is sufficient to form pores within membranes. Released myr-μ1N can also promote ISVP* formation in trans. Using thermal inactivation as a readout for ISVP-to-ISVP* conversion, we demonstrate that lipids render ISVPs less thermostable in a virus concentration-dependent manner. Under conditions in which neither lipids alone nor myr-μ1N alone promotes ISVP-to-ISVP* conversion, myr-μ1N induces particle uncoating when lipids are present. These data suggest that the pore-forming activity and the ISVP*-promoting activity of myr-μ1N are linked. Lipid-associated myr-μ1N interacts with ISVPs and triggers efficient ISVP* formation. The cooperativity between a reovirus component and lipids reveals a distinct virus-host interaction in which membranes can facilitate nonenveloped virus entry.
Footnotes
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* This work was supported by NIAID, National Institutes of Health Grant 1R01AI110637 (to P. D.). The authors declare that they have no conflicts of interest with the contents of this article. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
- Received July 8, 2016.
- Revision received November 14, 2016.
- © 2016 by The American Society for Biochemistry and Molecular Biology, Inc.
