Simian TRIM5α proteins reduce replication of herpes simplex virus

Reszka, Natalia; Zhou, Chunxia; Song, Byeongwoon; Sodroski, Joseph; Knipe, David M.

doi:10.1016/j.virol.2009.11.041

Cited by 26 publications

(27 citation statements)

References 55 publications

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“…Importantly, this does support the idea that there are cognate viral forms that correspond to different host immunity alleles. It was recently found that TRIM5α also restricts herpes simplex virus, but that this effect is highly virus strain-specific [67]. This is again consistent with viral populations having cognate polymorphisms that exhibit escape from certain host alleles.…”

Section: Rock-paper-scissors: Are Arms Races Cyclic?mentioning

confidence: 55%

Two-stepping through time: mammals and viruses

Meyerson

Sawyer

2011

Trends in Microbiology

133

140

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Recent studies have identified ancient virus genomes preserved as fossils within diverse animal genomes. These fossils have led to the revelation that a broad range of mammalian virus families are older and more ubiquitous than previously appreciated. Long-term interactions between viruses and their hosts often develop into genetic arms races, where both parties continually jockey for evolutionary dominance. It is difficult to imagine how mammalian hosts have kept pace in the evolutionary race against rapidly evolving viruses over large expanses of time, given their much slower evolutionary rates. However, recent data has begun to reveal the evolutionary strategy of slowly-evolving hosts. We review these data, and suggest a modified arms race model where the evolutionary possibilities of viruses are relatively constrained. Such a model could allow more accurate forecasting of virus evolution.

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Section: Rock-paper-scissors: Are Arms Races Cyclic?mentioning

confidence: 55%

Two-stepping through time: mammals and viruses

Meyerson

Sawyer

2011

Trends in Microbiology

133

140

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“…Our present data demonstrating that herpesvirus capsids become ubiquitinated and subject to proteasomal degradation strongly suggest that the herpesvirus capsid is also recognized within the cytosol. Interestingly, Trim5α has recently been reported to inhibit HSV-1 and -2 replication at an early stage of the infection cycle (48), suggesting a role for this or a related protein in cytosolic sensing of herpesvirus capsids. Early work by Sodeik et al demonstrated that empty HSV-1 capsids (indicating delivery of DNA to the nucleus) start to accumulate inside Vero cells about 1 h post infection, and reach a level of 60% of all intracellular capsids at 4 h post infection (49).…”

Section: Discussionmentioning

confidence: 99%

Proteasomal Degradation of Herpes Simplex Virus Capsids in Macrophages Releases DNA to the Cytosol for Recognition by DNA Sensors

Horan

Hansen

Jakobsen

et al. 2013

The Journal of Immunology

180

211

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The innate immune system is important for control of infections, including herpesvirus infections. Intracellular DNA potently stimulates antiviral IFN responses. It is known that plasmacytoid dendritic cells sense herpesvirus DNA in endosomes via TLR9, and that non-immune tissue cells can sense herpesvirus DNA in the nucleus. However, it remains unknown how and where myeloid cells, like macrophages and conventional dendritic cells, detect infections with herpesviruses. Here we demonstrate that the HSV-1 capsid was ubiquitinated in the cytosol and degraded by the proteasome, hence releasing genomic DNA into the cytoplasm for detection by DNA sensors. In this context, the DNA sensor IFI16 is important for induction of IFN-β in human macrophages after infection with HSV-1 and CMV. Viral DNA localized to the same cytoplasmic regions as IFI16, with DNA sensing being independent of viral nuclear entry. Thus, proteasomal degradation of herpesvirus capsids releases DNA to the cytoplasm for recognition by DNA sensors.

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“…Moreover, several TRIM proteins were proposed to restrict human immunodeficiency virus (HIV) or murine leukemia viruses (MLV) replication upon overexpression in vitro [3,5,7]. In addition to the antiviral activity to RNA virus, TRIM21 and TRIM5a were also found to exert their antiviral roles against DNA viruses [8].…”

Section: Introductionmentioning

confidence: 99%

Grouper TRIM13 exerts negative regulation of antiviral immune response against nodavirus

Huang

Yang

et al. 2016

Fish & Shellfish Immunology

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The tripartite motif (TRIM)-containing proteins have attracted particular attention to their multiple functions in different biological processes. TRIM13, a member of the TRIM family, is a RING domain-containing E3 ubiquitin ligase which plays critical roles in diverse cellular processes including cell death, cancer and antiviral immunity. In this study, a TRIM13 homolog from orange spotted grouper, Epinephelus coioides (EcTRIM13) was cloned and characterized. The full-length of EcTRIM13 cDNA encoded a polypeptide of 399 amino acids which shared 81% identity with TRIM13 homolog from large yellow croaker (Larimichthys crocea). Amino acid alignment analysis showed that EcTRIM13 contained conserved RING finger and B-box domain. Expression patterns analysis indicated that EcTRIM13 was abundant in liver, spleen, kidney, intestine and gill. Moreover, the transcript of EcTRIM13 in grouper spleen was differently regulated after injection with Singapore grouper iridovirus (SGIV) or polyinosin-polycytidylic acid (poly I:C). Under fluorescence microscopy, we observed the tubular structure in wild type EcTRIM13 transfected cells, but the RING domain mutant resulted in the fluorescence distribution was changed and the bright punctate fluorescence was evenly situated throughout the cytoplasm, suggesting that the RING domain was essential for its accurate localization. Overexpression of EcTRIM13 in vitro obviously increased the replication of red spotted grouper nervous necrosis virus (RGNNV), and the enhancing effect of EcTRIM13 on virus replication was affected by the RING domain. Furthermore, the ectopic expression of EcTRIM13 not only negatively regulated the interferon promoter activity induced by interferon regulator factor (IRF) 3, IRF7, and melanoma differentiation-associated protein 5 (MDA5), but also decreased the expression of several interferon related factors. In addition, the overexpression of EcTRIM13 also differently regulated the transcription of pro-inflammatory factors. Together, our results firstly demonstrated that fish TRIM13 exerted negative regulation of antiviral response against nodavirus infection.

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Simian TRIM5α proteins reduce replication of herpes simplex virus

Cited by 26 publications

References 55 publications

Two-stepping through time: mammals and viruses

Two-stepping through time: mammals and viruses

Proteasomal Degradation of Herpes Simplex Virus Capsids in Macrophages Releases DNA to the Cytosol for Recognition by DNA Sensors

Grouper TRIM13 exerts negative regulation of antiviral immune response against nodavirus

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