Date Published: September 20, 2018
Publisher: Public Library of Science
Author(s): Anthony R. Dawson, Andrew Mehle, Matthew J. Evans.
Precise coordination of cellular processes requires prompt specification of protein function in response to various stimuli. This specification includes regulating protein abundance, localization, catalysis, and binding. Post-translational modifications (PTMs) provide cells the plasticity for dynamic and reversible control of protein function. Viral infections provide an exciting lens through which to study PTMs, since PTMs contribute to both cellular responses to infection and viral hijacking of the host. PTMs enhance the already multifunctional nature of viral proteins and offer another level of functional diversity within limited genetic space. Influenza virus protein functions are fine-tuned by diverse types of PTMs, including phosphorylation, ubiquitination, SUMOylation, neddylation, ISGylation, glycosylation, ADP-ribosylation, palmitoylation, and acetylation. All of the major viral proteins are subject to at least one type of PTM. Additionally, as influenza viruses encode no known protein-modifying enzymes, all of these PTMs are mediated by host machinery. Here, we use influenza virus and its proteins as exemplars for how PTMs impact virus replication (Fig 1).