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 language | English (US) |
|---|---|
| Article number | 23 |
| Journal | Vaccines |
| Volume | 5 |
| Issue number | 3 |
| DOIs | |
| State | Published - Sep 1 2017 |
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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 journal › Article
}
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 -