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Vaccines 2017, 5(3), 23; doi:10.3390/vaccines5030023

The TRIMendous Role of TRIMs in Virus–Host Interactions

1
Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX 77555, USA
2
Institute for Human Infections and Immunity, University of Texas Medical Branch, Galveston, TX 77555, USA
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editors: Angela L. Rasmussen and Juliet Morrison
Received: 8 July 2017 / Revised: 9 August 2017 / Accepted: 17 August 2017 / Published: 22 August 2017
(This article belongs to the Special Issue Host Responses to Viral Infection)
View Full-Text   |   Download PDF [3593 KB, uploaded 22 August 2017]   |  

Abstract

The innate antiviral response is integral in protecting the host against virus infection. Many proteins regulate these signaling pathways including ubiquitin enzymes. The ubiquitin-activating (E1), -conjugating (E2), and -ligating (E3) enzymes work together to link ubiquitin, a small protein, onto other ubiquitin molecules or target proteins to mediate various effector functions. The tripartite motif (TRIM) protein family is a group of E3 ligases implicated in the regulation of a variety of cellular functions including cell cycle progression, autophagy, and innate immunity. Many antiviral signaling pathways, including type-I interferon and NF-κB, are TRIM-regulated, thus influencing the course of infection. Additionally, several TRIMs directly restrict viral replication either through proteasome-mediated degradation of viral proteins or by interfering with different steps of the viral replication cycle. In addition, new studies suggest that TRIMs can exert their effector functions via the synthesis of unconventional polyubiquitin chains, including unanchored (non-covalently attached) polyubiquitin chains. TRIM-conferred viral inhibition has selected for viruses that encode direct and indirect TRIM antagonists. Furthermore, new evidence suggests that the same antagonists encoded by viruses may hijack TRIM proteins to directly promote virus replication. Here, we describe numerous virus–TRIM interactions and novel roles of TRIMs during virus infections. View Full-Text
Keywords: innate immunity; virus infection; tripartite motif (TRIM); E3-ubiquitin ligase; ubiquitin; viral antagonism; type-I interferons; unanchored polyubiquitin innate immunity; virus infection; tripartite motif (TRIM); E3-ubiquitin ligase; ubiquitin; viral antagonism; type-I interferons; unanchored polyubiquitin
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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. (CC BY 4.0).

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MDPI and ACS Style

van Tol, S.; Hage, A.; Giraldo, M.I.; Bharaj, P.; Rajsbaum, R. The TRIMendous Role of TRIMs in Virus–Host Interactions. Vaccines 2017, 5, 23.

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