期刊
CELL HOST & MICROBE
卷 18, 期 2, 页码 221-232出版社
CELL PRESS
DOI: 10.1016/j.chom.2015.07.007
关键词
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资金
- National Institutes of Health [R01AI081759, R01AI072490, T32AI049820, T32AI060525]
- Burroughs Wellcome Investigators in the Pathogenesis of Infectious Disease award
- Plotkin Endowed Chair in infectious Diseases at the Children's Hospital of Philadelphia
- ARCS Foundation Scholar Award
Receptor interacting protein kinase-3 (RIP3) is an essential kinase for necroptotic cell death signaling and has been implicated in antiviral cell death signaling upon DNA virus infection. Here, we performed high-throughput RNAi screening and identified RIP3 as a positive regulator of coxsackievirus B3 (CVB) replication in intestinal epithelial cells (IECs). RIP3 regulates autophagy, a process utilized by CVB for viral replication factory assembly, and depletion of RIP3 inhibits autophagic flux and leads to the accumulation of autophagosomes and amphisomes. Additionally, later in infection, RIP3 is cleaved by the CVB-encoded cysteine protease 3C pro, which serves to abrogate RIP3-mediated necrotic signaling and induce a nonnecrotic form of cell death. Taken together, our results show that temporal targeting of RIP3 allows CVB to benefit from its roles in regulating autophagy while inhibiting the induction of necroptotic cell death.
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