The equine arteritis virus induces apoptosis via caspase-8 and mitochondria-dependent caspase-9 activation.

Abstract

We have previously showed that equine arteritis virus (EAV), an arterivirus, induces apoptosis in vitro. To determine the caspase activation pathways involved in EAV-induced apoptosis, target cells were treated with peptide inhibitors of apoptosis Z-VAD-FMK (pan-caspase inhibitor), Z-IETD-FMK (caspase-8-specific inhibitor) or Z-LEHD-FMK (caspase-9-specific inhibitor) 4 h prior to infection with the EAV T1329 Canadian isolate. Significant inhibition of apoptosis was obtained with all peptide inhibitors used. Furthermore, apoptosis was inhibited in cells expressing the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase (HSV2-R1) or hsp70, two proteins which are known to inhibit apoptosis associated with caspase-8 activation and cytochrome c release-dependent caspase-9 activation, respectively. Given the activation of Bid and the translocation of cytochrome c within the cytoplasm, the overall results indicate that EAV induces apoptosis initiated by caspase-8 activation and subsequent mitochondria-dependent caspase-9 activation.

• Authors: Marie-Claude St-Louis, Denis Archambault
• Journal: Virology (Virology) Vol. 367 Issue 1 Pg. 147-55 (Oct 10 2007) ISSN: 0042-6822 [Print] United States
• PMID: 17583760 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• BH3 Interacting Domain Death Agonist Protein
• bcl-2-Associated X Protein
• Cytochromes c
• Caspase 8
• Caspase 9

Topics

• Animals
• Apoptosis (physiology)
• BH3 Interacting Domain Death Agonist Protein (metabolism)
• Caspase 8 (metabolism)
• Caspase 9 (metabolism)
• Chlorocebus aethiops
• Cytochromes c (metabolism)
• Enzyme Activation
• Equartevirus (pathogenicity)
• Flow Cytometry
• Mitochondria (enzymology)
• Vero Cells
• bcl-2-Associated X Protein (metabolism)