Direct cleavage of caspase-8 by herpes simplex virus 1 tegument protein US11
The HSV-1 tegument protein Us11 counteracts the antiviral defense mechanisms by precluding the host protein shutoff. Previous works demonstrated that Us11 prevents heat-and staurosporine-induced apoptosis and inhibits autophagy. Therefore, in the present study, we investigated the hypothesis that HS...
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| Published in: | Scientific reports Vol. 12; no. 1; p. 12317 |
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| Abstract | The HSV-1 tegument protein Us11 counteracts the antiviral defense mechanisms by precluding the host protein shutoff. Previous works demonstrated that Us11 prevents heat-and staurosporine-induced apoptosis and inhibits autophagy. Therefore, in the present study, we investigated the hypothesis that HSV-1, through Us11, could recruit caspase-8, a key enzyme regulating programmed cell death. We first show that HSV-1 promotes the accumulation of caspase-8-p18 active fragments in both semi permissive THP-1 cells and fully permissive HEp-2 cells to HSV-1 replication. Using a recombinant virus R3630 (ΔUs11/ΔUs12) and a plasmid encoding Us11-recombinant protein we have proven that Us11 promotes p18 accumulation, which does not trigger the apoptotic signaling. Additional, in an in vitro model, we demonstrated that Us11-recombinant protein induces caspase-8-p18 cleavage by physically interacting with the caspase-8 recombinant protein. Finally, we found that, during HSV-1 replication, activated-caspase-8 cleaves Atg3 protein to potentially block autophagy and support its replication. |
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| AbstractList | Abstract The HSV-1 tegument protein Us11 counteracts the antiviral defense mechanisms by precluding the host protein shutoff. Previous works demonstrated that Us11 prevents heat-and staurosporine-induced apoptosis and inhibits autophagy. Therefore, in the present study, we investigated the hypothesis that HSV-1, through Us11, could recruit caspase-8, a key enzyme regulating programmed cell death. We first show that HSV-1 promotes the accumulation of caspase-8-p18 active fragments in both semi permissive THP-1 cells and fully permissive HEp-2 cells to HSV-1 replication. Using a recombinant virus R3630 (ΔUs11/ΔUs12) and a plasmid encoding Us11-recombinant protein we have proven that Us11 promotes p18 accumulation, which does not trigger the apoptotic signaling. Additional, in an in vitro model, we demonstrated that Us11-recombinant protein induces caspase-8-p18 cleavage by physically interacting with the caspase-8 recombinant protein. Finally, we found that, during HSV-1 replication, activated-caspase-8 cleaves Atg3 protein to potentially block autophagy and support its replication. The HSV-1 tegument protein Us11 counteracts the antiviral defense mechanisms by precluding the host protein shutoff. Previous works demonstrated that Us11 prevents heat-and staurosporine-induced apoptosis and inhibits autophagy. Therefore, in the present study, we investigated the hypothesis that HSV-1, through Us11, could recruit caspase-8, a key enzyme regulating programmed cell death. We first show that HSV-1 promotes the accumulation of caspase-8-p18 active fragments in both semi permissive THP-1 cells and fully permissive HEp-2 cells to HSV-1 replication. Using a recombinant virus R3630 (ΔUs11/ΔUs12) and a plasmid encoding Us11-recombinant protein we have proven that Us11 promotes p18 accumulation, which does not trigger the apoptotic signaling. Additional, in an in vitro model, we demonstrated that Us11-recombinant protein induces caspase-8-p18 cleavage by physically interacting with the caspase-8 recombinant protein. Finally, we found that, during HSV-1 replication, activated-caspase-8 cleaves Atg3 protein to potentially block autophagy and support its replication. |
| ArticleNumber | 12317 |
| Author | Velletri, Tania Pennisi, Rosamaria Sciortino, Maria Teresa Musarra-Pizzo, Maria Lombardo, Daniele |
| Author_xml | – sequence: 1 givenname: Maria surname: Musarra-Pizzo fullname: Musarra-Pizzo, Maria email: maria.musarrapizzo@unime.it organization: Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina – sequence: 2 givenname: Rosamaria surname: Pennisi fullname: Pennisi, Rosamaria organization: Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina – sequence: 3 givenname: Daniele surname: Lombardo fullname: Lombardo, Daniele organization: Division of Clinical and Molecular Hepatology, University Hospital ‘G. Martino’ of Messina – sequence: 4 givenname: Tania surname: Velletri fullname: Velletri, Tania organization: IFOM-Cogentech Società Benefit Srl – sequence: 5 givenname: Maria Teresa surname: Sciortino fullname: Sciortino, Maria Teresa email: mtsciortino@unime.it organization: Department of Chemical, Biological, Pharmaceutical and Environmental Sciences, University of Messina |
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| SubjectTerms | 631/326 631/326/596 Apoptosis Autophagy Caspase-8 Cell death Herpes simplex Herpes viruses Humanities and Social Sciences Kinases multidisciplinary Replication Science Science (multidisciplinary) Staurosporine Tegument Viral infections |
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| Title | Direct cleavage of caspase-8 by herpes simplex virus 1 tegument protein US11 |
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