Abstract
With no limiting membrane surrounding virions, nonenveloped viruses have no need for membrane fusion to gain access to intracellular replication compartments. Consequently, nonenveloped viruses do not encode membrane fusion proteins. The only exception to this dogma is the fusogenic reoviruses that encode fusion-associated small transmembrane (FAST) proteins that induce syncytium formation. FAST proteins are the smallest viral membrane fusion proteins and, unlike their enveloped virus counterparts, are nonstructural proteins that evolved specifically to induce cell-to-cell, not virus-cell, membrane fusion. This distinct evolutionary imperative is reflected in structural and functional features that distinguish this singular family of viral fusogens from all other protein fusogens. These rudimentary fusogens comprise specific combinations of different membrane effector motifs assembled into small, modular membrane fusogens. FAST proteins offer a minimalist model to better understand the ubiquitous process of protein-mediated membrane fusion and to reveal novel mechanisms of nonenveloped virus dissemination that contribute to virulence.
| Original language | English |
|---|---|
| Pages (from-to) | 341-363 |
| Number of pages | 23 |
| Journal | Annual Review of Virology |
| Volume | 6 |
| DOIs | |
| Publication status | Published - Sept 29 2019 |
Bibliographical note
Funding Information:The author gratefully acknowledges the accomplishments of the numerous students, postdoctoral fellows, and research associates with whom it has been his privilege to collaborate. Their efforts, both intellectual and technical, provided the foundations for this review. Research conducted in the author's laboratory was supported by the Canadian Institutes of Health Research and the Natural Sciences and Engineering Research Council of Canada.
Publisher Copyright:
© 2019 by Annual Reviews. All rights reserved.
ASJC Scopus Subject Areas
- Virology