Proteomics - Clinical Applications
Proteomics - Clinical Applications
5 years ago

Ubiquitin-Conjugating Enzyme E2 L3 is Downregulated by the Chikungunya Virus nsP2 Protease

Prasert Auewarakul, Suwipa Ramphan, Atichat Kuadkitkan, Duncan R. Smith, Sittiruk Roytrakul, Chonticha Saisawang, Albert J. Ketterman, Sukathida Ubol, Duangnapa Kovanich, Sarawut Khongwichit
Purpose Chikungunya virus (CHIKV) is a mosquito transmitted alphavirus that causes chikungunya fever in humans. The CHIKV nonstructural protein 2 (nsP2) is a multifunctional protein that additionally modulates the host cell to dampen the innate immune response and inhibit other cellular processes. Experimental design To further investigate the interactions of nsP2 with host cells, the protease domain of CHIKV nsP2 (nsP2-pro) was transfected into Hela cells, and differential protein expression was detected by 2-dimension (2D) polyacrylamide gel electrophoresis. Results A total of 21 differentially regulated (6 upregulated, 15 downregulated) spots were observed, of which 5 were identified by mass spectrometry. The downregulation of one of the identified proteins, ubiquitin-conjugating enzyme E2 L3 (UBE2L3) was confirmed by western blotting of both nsP2-pro transfection and CHIKV natural infection, and the downregulation of UBE2L3 was additionally shown to require an enzymatically active nsP2 protease domain. Transfection of full length UBE2L3 into HEK293T/17 cells prior to CHIKV infection reduced levels of infection and E protein expression but did not alter RNA genome levels. Conclusion These results suggest that UBE2L3 is a cellular target of the CHIKV nsP2 protease, and this possibly mediates the pathogenesis of chikungunya fever. This article is protected by copyright. All rights reserved

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1002/prca.201700020

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