Review
Version 1
Preserved in Portico This version is not peer-reviewed
A Balancing Act: The Viral-Host Battle over RBPs
Version 1
: Received: 15 December 2023 / Approved: 18 December 2023 / Online: 18 December 2023 (11:00:00 CET)
A peer-reviewed article of this Preprint also exists.
Bermudez, Y.; Hatfield, D.; Muller, M. A Balancing Act: The Viral–Host Battle over RNA Binding Proteins. Viruses 2024, 16, 474. Bermudez, Y.; Hatfield, D.; Muller, M. A Balancing Act: The Viral–Host Battle over RNA Binding Proteins. Viruses 2024, 16, 474.
Abstract
A defining feature of a productive infection is the co-opting of host cell resources for viral replication. Despite their repertoire of molecular functions, viruses subvert host defenses to take control of cellular factors such as RNA binding proteins (RBPs). RBPs are involved in virtually all steps of mRNA life forming ribonucleoprotein complexes (mRNPs) in a highly ordered and regulated process to control RNA fate and stability in the cell. Thus, the hallmark of this viral takeover is to reshape RNA fate in the cell to modulate host gene expression and evade immune responses. Here we provide an extensive review of work in this area, particularly how the host-viral interplay influences RBP functions to modulate the host cell. Overall, in this review, we highlight the myriad of ways RBPs can regulate RNA stability in either a pro-viral or antiviral manner by gathering novel insights gained from research studies in this field.
Keywords
RNA binding proteins; protein-RNA interactions; RNA decay; RNA granules; viruses
Subject
Biology and Life Sciences, Virology
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Comments (0)
We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.
Leave a public commentSend a private comment to the author(s)
* All users must log in before leaving a comment