HSV1 RIR1 binds RIPK3

Stable Identifier
Reaction [binding]
Homo sapiens
Related Species
Human herpesvirus 1
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During infection in human cells, herpes simplex virus (HSV)-1 and HSV-2 modulate cell death pathways using the large subunit (R1) of viral ribonucleotide reductase (RIR1 or UL39) (Dufour F et al. 2011; Guo H et al. 2015; Yu X et al. 2016; Ali M et al.2019). The N-terminal region of RIR1 protein carrying the RIP homotypic interaction motif (RHIM)-like element is sufficient for RHIM-dependent interaction with receptor‐interacting protein kinase 1 (RIPK1) and receptor‐interacting protein kinase 3 (RIPK3) thus inhibiting the interaction between RIPK1 and RIPK3 (Guo H et al. 2015; Yu X et al. 2015). An intact RHIM is required for the interaction between RIPK1 and RIPK3 that occurs downstream of tumour necrosis factor receptor 1 (TNFR1) activation during the programmed cell death response known as necroptosis (Sun X et al. 2002). In addition, the large carboxyl-terminal region of HSV RIR1 protein mediates the binding to caspase 8 (CASP8) (Dufour F et al. 2011; Guo H et al. 2015). HSV RIR1 is thought to block necroptosis in infected human cells by interactions with RIPK1, RIPK3 and CASP8 (Guo H et al. 2015; Mocarski ES et al. 2015).

Literature References
PubMed ID Title Journal Year
25674983 Herpes simplex virus suppresses necroptosis in human cells

Guo, H, Omoto, S, Harris, PA, Finger, JN, Bertin, J, Gough, PJ, Kaiser, WJ, Mocarski, ES

Cell Host Microbe 2015
26559832 Herpes Simplex Virus 1 (HSV-1) and HSV-2 Mediate Species-Specific Modulations of Programmed Necrosis through the Viral Ribonucleotide Reductase Large Subunit R1

Yu, X, Li, Y, Chen, Q, Su, C, Zhang, Z, Yang, C, Hu, Z, Hou, J, Zhou, J, Gong, L, Jiang, X, Zheng, C, He, S

J. Virol. 2016
Event Information
Name Identifier Synonyms
viral infectious disease DOID:934 Viral disease, virus infection, virus infection
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