The TRIMendous role of TRIMs in virus-host interactions

Sarah van Tol, Adam Hage, Maria Giraldo Giraldo, Preeti Bharaj, Ricardo Rajsbaum Gorodezky

Research output: Contribution to journalArticle

17 Citations (Scopus)

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.

Original languageEnglish (US)
Article number23
JournalVaccines
Volume5
Issue number3
DOIs
StatePublished - Sep 1 2017

Fingerprint

Ubiquitin
Polyubiquitin
Viruses
Virus Diseases
Antiviral Agents
Interferon Type I
Proteins
Ubiquitin-Protein Ligases
Autophagy
Viral Proteins
Proteasome Endopeptidase Complex
Enzymes
Virus Replication
Innate Immunity
Cell Cycle
Infection
Tripartite Motif Proteins

Keywords

  • E3-ubiquitin ligase
  • Innate immunity
  • Tripartite motif (TRIM)
  • Type-I interferons
  • Ubiquitin
  • Unanchored polyubiquitin
  • Viral antagonism
  • Virus infection

ASJC Scopus subject areas

  • Immunology
  • Pharmacology
  • Drug Discovery
  • Pharmacology (medical)
  • Infectious Diseases

Cite this

The TRIMendous role of TRIMs in virus-host interactions. / van Tol, Sarah; Hage, Adam; Giraldo Giraldo, Maria; Bharaj, Preeti; Rajsbaum Gorodezky, Ricardo.

In: Vaccines, Vol. 5, No. 3, 23, 01.09.2017.

Research output: Contribution to journalArticle

@article{0c54ebaf56fd4a65a825216fd58f1469,
title = "The TRIMendous role of TRIMs in virus-host interactions",
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.",
keywords = "E3-ubiquitin ligase, Innate immunity, Tripartite motif (TRIM), Type-I interferons, Ubiquitin, Unanchored polyubiquitin, Viral antagonism, Virus infection",
author = "{van Tol}, Sarah and Adam Hage and {Giraldo Giraldo}, Maria and Preeti Bharaj and {Rajsbaum Gorodezky}, Ricardo",
year = "2017",
month = "9",
day = "1",
doi = "10.3390/vaccines5030023",
language = "English (US)",
volume = "5",
journal = "Vaccines",
issn = "2076-393X",
publisher = "Multidisciplinary Digital Publishing Institute (MDPI)",
number = "3",

}

TY - JOUR

T1 - The TRIMendous role of TRIMs in virus-host interactions

AU - van Tol, Sarah

AU - Hage, Adam

AU - Giraldo Giraldo, Maria

AU - Bharaj, Preeti

AU - Rajsbaum Gorodezky, Ricardo

PY - 2017/9/1

Y1 - 2017/9/1

N2 - 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.

AB - 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.

KW - E3-ubiquitin ligase

KW - Innate immunity

KW - Tripartite motif (TRIM)

KW - Type-I interferons

KW - Ubiquitin

KW - Unanchored polyubiquitin

KW - Viral antagonism

KW - Virus infection

UR - http://www.scopus.com/inward/record.url?scp=85028727543&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85028727543&partnerID=8YFLogxK

U2 - 10.3390/vaccines5030023

DO - 10.3390/vaccines5030023

M3 - Article

AN - SCOPUS:85028727543

VL - 5

JO - Vaccines

JF - Vaccines

SN - 2076-393X

IS - 3

M1 - 23

ER -