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Details on Person During infection in human cells, herpes simplex virus 1 (HSV...
| Class:Id | Summation:9687464 |
|---|---|
| _displayName | During infection in human cells, herpes simplex virus 1 (HSV... |
| _timestamp | 2020-07-17 23:01:45 |
| created | [InstanceEdit:9687477] Shamovsky, Veronica, 2020-05-09 |
| literatureReference | [LiteratureReference:9687450] Herpes simplex virus 1 ICP6 impedes TNF receptor 1-induced necrosome assembly during compartmentalization to detergent-resistant membrane vesicles [LiteratureReference:5364097] Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3 [LiteratureReference:9687472] Herpes Simplex Virus 1 (HSV-1) and HSV-2 Mediate Species-Specific Modulations of Programmed Necrosis through the Viral Ribonucleotide Reductase Large Subunit R1 [LiteratureReference:9687474] Herpes simplex virus suppresses necroptosis in human cells [LiteratureReference:9687481] Necroptosis: The Trojan horse in cell autonomous antiviral host defense [LiteratureReference:9687460] The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8 |
| modified | [InstanceEdit:9696113] Shamovsky, Veronica, 2020-07-17 |
| text | During infection in human cells, herpes simplex virus 1 (HSV1) and HSV2 modulate cell death pathways using the large subunit (R1) of viral ribonucleotide reductase (RIR1 or UL39) proteins (Dufour F et al. 2011; Guo H et al. 2015; Yu X et al. 2016; Ali M et al. 2019). The HSV1 and HSV2 RIR1 proteins suppress death receptor-dependent apoptosis by interacting with death effector domains of caspase 8 (CASP8) via a conserved C-terminal ribonucleotide reductase (RNR) domain (Dufour F et al. 2011). The ability of HSV1 RIR1 and HSV2 RIR1 to bind CASP8 is integral to their suppression activity against necroptosis in human cells. Necroptosis complements apoptosis as a host defense pathway to stop virus infection and is mediated by the interaction between receptor‐interacting protein kinase 1 (RIPK1) and RIPK3 that occurs downstream of tumor necrosis factor receptor 1 (TNFR1) activation during the programmed cell death response (Sun X et al. 2002). The N-terminal region of HSV1 and HSV2 RIR1 proteins carrying the RIP homotypic interaction motif (RHIM)-like element is sufficient for RHIM-dependent interaction with RIPK1 and RIPK3 thus inhibiting the interaction between RIPK1 and RIPK3 (Guo H et al. 2015; Yu X et al. 2015). HSV1 RIR1 and HSV2 RIR1 are thought to block the programmed cell death responses in infected human cells by interactions with RIPK1, RIPK3 and CASP8 (Guo H et al. 2015; Mocarski ES et al. 2015). |
| (summation) | [Reaction:9687458] HSV1 RIR1 binds CASP8 [Homo sapiens] |
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