Caspase activation in equine influenza virus induced apoptotic cell death.
Abstract: Equine influenza virus (EIV) is the leading cause of acute respiratory infection in horses worldwide. In recent years, the precise mechanism by which influenza infection kills host cells is being re-evaluated. In this report, we examined whether caspases, a group of intracellular proteases, are activated following EIV infection and contribute to EIV-mediated cell death. Western blotting analysis indicated that a nuclear target of caspase-3, poly(ADP-ribose) polymerase (PARP) was proteolytically cleaved in EIV-infected MDCK cells, but not in mock-infected cells. In comparison with caspase-3 specific inhibitor Ac-DEVD-CHO, a general caspase inhibitor Boc-D-FMK provided much stronger inhibition of EIV-induced cytopathic effect and apoptosis. Our results suggest that EIV may activate more than one caspase. Caspase activation and cleavage of its cellular targets may play a critical role in EIV-mediated cytotoxicity.
Publication Date: 2001-12-26 PubMed ID: 11750143DOI: 10.1016/s0378-1135(01)00468-0Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- Non-P.H.S.
- Review
Summary
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This study examines how the equine influenza virus (EIV), a leading cause of respiratory infections in horses, triggers cell death through the activation of protease enzymes, known as caspases.
Context and Objective
- The objective of this research was to investigate the role of caspases, enzymes that instigate apoptosis (programed cell death), in the progression of Equine Influenza Virus (EIV) infection.
- This was prompted by the necessity of understanding the exact mechanisms of how influenza viruses lead to cell death in hosts.
Methodology
- The researchers used Western blotting analysis (a technique to detect specific proteins in a sample) to determine if caspase-3, a particular caspase enzyme, was activated following EIV infection.
- They examined the presence of proteolytic cleavage (breakdown of proteins) in the cells following infection by EIV. The target of this cleavage process was poly(ADP-ribose) polymerase (PARP), characterized as a nuclear target of caspase-3.
- The effect of specific inhibitors for caspase activity, particularly a caspase-3-specific inhibitor (Ac-DEVD-CHO) and a general caspase inhibitor (Boc-D-FMK), were also studied in relation to EIV’s impact on cells.
Findings
- The researchers found that PARP was proteolytically cleaved in cells infected by EIV, which was not observed in non-infected cells, suggesting caspase activation following EIV infection.
- The general caspase inhibitor was shown to strongly inhibit EIV-induced cytopathic effect (visible effects of viral infection) and apoptosis, suggesting that more than just caspase-3 could be activated by EIV.
- The specific inhibitor of caspase-3 also reduced EIV-mediated cell death, though not as effectively as the general inhibitor, supporting the idea that multiple caspases may be implicated in this process.
Conclusion
- The results of this study suggest that EIV may trigger the activation of more than one type of caspase in infected cells.
- This activation and the subsequent breakdown of cellular targets by the caspases may play a crucial role in the cell death caused by an EIV infection.
Cite This Article
APA
Lin C, Holland RE, Donofrio JC, McCoy MH, Tudor LR, Chambers TM.
(2001).
Caspase activation in equine influenza virus induced apoptotic cell death.
Vet Microbiol, 84(4), 357-365.
https://doi.org/10.1016/s0378-1135(01)00468-0 Publication
Researcher Affiliations
- Department of Veterinary Science, The Maxwell H. Gluck Equine Research Center, University of Kentucky, Lexington, KY 40546-0099, USA. chengbin.lin@spcorp.com
MeSH Terms
- Animals
- Apoptosis / physiology
- Caspase Inhibitors
- Caspases / metabolism
- Cell Line
- Enzyme Activation
- Enzyme Inhibitors / pharmacology
- Horse Diseases / enzymology
- Horse Diseases / pathology
- Horses
- Influenza A virus / enzymology
- Orthomyxoviridae Infections / enzymology
- Orthomyxoviridae Infections / pathology
- Orthomyxoviridae Infections / veterinary
- Virus Replication
Citations
This article has been cited 14 times.- Anderson C, Baha H, Boghdeh N, Barrera M, Alem F, Narayanan A. Interactions of Equine Viruses with the Host Kinase Machinery and Implications for One Health and Human Disease.. Viruses 2023 May 13;15(5).
- Peng S, Guo C, Wu S, Duan Z. Isolation, characterization and anti-UVB irradiation activity of an extracellular polysaccharide produced by Lacticaseibacillus rhamnosus VHPriobi O17.. Heliyon 2022 Oct;8(10):e11125.
- Gonzalez-Obando J, Forero JE, Zuluaga-Cabrera AM, Ruiz-Saenz J. Equine Influenza Virus: An Old Known Enemy in the Americas.. Vaccines (Basel) 2022 Oct 14;10(10).
- Singh RK, Dhama K, Karthik K, Khandia R, Munjal A, Khurana SK, Chakraborty S, Malik YS, Virmani N, Singh R, Tripathi BN, Munir M, van der Kolk JH. A Comprehensive Review on Equine Influenza Virus: Etiology, Epidemiology, Pathobiology, Advances in Developing Diagnostics, Vaccines, and Control Strategies.. Front Microbiol 2018;9:1941.
- Li XQ, Cai LM, Liu J, Ma YL, Kong YH, Li H, Jiang M. Liquiritin suppresses UVB‑induced skin injury through prevention of inflammation, oxidative stress and apoptosis through the TLR4/MyD88/NF‑κB and MAPK/caspase signaling pathways.. Int J Mol Med 2018 Sep;42(3):1445-1459.
- Zhou P, Tu L, Lin X, Hao X, Zheng Q, Zeng W, Zhang X, Zheng Y, Wang L, Li S. cfa-miR-143 Promotes Apoptosis via the p53 Pathway in Canine Influenza Virus H3N2-Infected Cells.. Viruses 2017 Nov 25;9(12).
- Chen L, Jin T, Zhu K, Piao Y, Quan T, Quan C, Lin Z. PI3K/mTOR dual inhibitor BEZ235 and histone deacetylase inhibitor Trichostatin A synergistically exert anti-tumor activity in breast cancer.. Oncotarget 2017 Feb 14;8(7):11937-11949.
- Cai Z, Liang P, Xuan J, Wan J, Guo H. ECRG4 as a novel tumor suppressor gene inhibits colorectal cancer cell growth in vitro and in vivo.. Tumour Biol 2016 Jul;37(7):9111-20.
- Liu XP, Huang D, Tan WS, Luo J, Chen Z. Overcoming nutrient limitations for cell-based production of influenza vaccine.. Hum Vaccin Immunother 2015;11(7):1685-8.
- Lin C, Holland RE Jr, McCoy MH, Donofrio-Newman J, Vickers ML, Chambers TM. Infectivity of equine H3N8 influenza virus in bovine cells and calves.. Influenza Other Respir Viruses 2010 Nov;4(6):357-61.
- Qian S, Cao J, Yan Y, Sun M, Zhu H, Hu Y, He Q, Yang B. SMT-A07, a 3-(Indol-2-yl) indazole derivative, induces apoptosis of leukemia cells in vitro.. Mol Cell Biochem 2010 Dec;345(1-2):13-21.
- Seo YJ, Blake C, Alexander S, Hahm B. Sphingosine 1-phosphate-metabolizing enzymes control influenza virus propagation and viral cytopathogenicity.. J Virol 2010 Aug;84(16):8124-31.
- Yang W, Qu S, Liu Q, Zheng C. Avian influenza virus A/chicken/Hubei/489/2004 (H5N1) induces caspase-dependent apoptosis in a cell-specific manner.. Mol Cell Biochem 2009 Dec;332(1-2):233-41.
- Wurzer WJ, Planz O, Ehrhardt C, Giner M, Silberzahn T, Pleschka S, Ludwig S. Caspase 3 activation is essential for efficient influenza virus propagation.. EMBO J 2003 Jun 2;22(11):2717-28.
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