Journal
FASEB JOURNAL
Volume 32, Issue 12, Pages 6706-6723Publisher
FEDERATION AMER SOC EXP BIOL
DOI: 10.1096/fj.201701351
Keywords
3A; protein interaction; innate immunity; cyclosporine A
Categories
Funding
- Facility Center Department, Lanzhou Veterinary Research Institute
- National Natural Sciences Foundation of China [U1501213, 31672585]
- Gansu Science Foundation [1606RJYA280, 1606RJDA313]
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Foot-and-mouth disease (FMD) is a highly contagious virus that affects cloven-hoofed animals. To understand better the role of nonstructural protein 2B of the causative agent FMD virus (FMDV) in the process of virus replication, we identified a porcine host protein, cyclophilin A (CypA), which interacts with FMDV 2B. The 2B-CypA interaction was confirmed by coimmunoprecipitation and GST pull-down assays. CypA showed antiviral functions during FMDV infection. Overexpression of CypA decreased FMDV leader protein (L-pro) and 3A at protein levels. CypA-induced reduction of L-pro enhanced the synthesis of host proteins and increased the integrality of host eukaryotic translation initiation factor (eIF)-4 (eIF4G). The reduction of L-pro and 3A was dependent on the proteasome pathway. No interaction was identified between CypA and L-pro or 3A. However, CypA-induced reduction of L-pro and 3A was suppressed by 2B, and disruption of 2B-CypA interaction impaired this inhibitive effect induced by 2B. In summary, our findings identify the antiviral role of CypA against FMDV and provide key insights into how FMDV antagonizes host antiviral response by 2B protein.Liu, H., Xue, Q., Cao, W., Yang, F., Ma, L., Liu, W., Zhang, K., Liu, X., Zhu, Z., Zheng, H. Foot-and-mouth disease virus nonstructural protein 2B interacts with cyclophilin A, modulating virus replication.
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