INTERACTION BETWEEN OV20.0 AND ADENOSINE DEAMINASES ACTING ON RNA 1

MUIR > Graduate Institute of Health Care > Department of Beauty Science > Papers > Item 987654321/3417

Please use this identifier to cite or link to this item: http://ir.meiho.edu.tw/ir/handle/987654321/3417

Title:	INTERACTION BETWEEN OV20.0 AND ADENOSINE DEAMINASES ACTING ON RNA 1
Authors:	Liao, Guan-Ru;Lin, Fong-Yuan;Yeu-Yang;Tseng;Hsu, Wei-Li
Keywords:	ADAR1;orf virus;OV20.0
Date:	2017-11-03
Issue Date:	2017-11-08T03:37:05Z (UTC)
Abstract:	Objectives: Orf virus (ORFV) OV20.0 is an important virulent factor. By interacting with protein kinase R (PKR) and its activator, namely PACT, OV20.0 inhibits PKR activation to promote virus replication. OV20.0, PKR and PACT all harbor dsRNA binding domains (DRBDs) and are classified as dsRNA binding proteins (DRBPs). It has been proposed that DRBPs regulate cell physiology by formation of protein dimer. A DRBP, designated adenosine deaminases acting on RNA 1 (ADAR1), catalyzes deamination of adenosine (A) to produce inosine (I) in dsRNA substrate in nucleus. Due to its nature of binding dsRNA, we postulated that OV20.0 possibly interacts with ADAR1. Therefore, we studied the impact of OV20.0 on cellular function of ADAR1 and their effects on ORFV pathogenesis. Methods: Immunoprecipitation was performed to identify cellular proteins interacting with OV20.0. A series of constructs containing deletions of individual functional domains were used to determine the minimal criterial for intermolecular interaction are determined. To further confirm their cellular distribution, transient expression of GFP-tagged OV20.0 and mCherry-tagged ADAR1 followed by immunofluorescence assay was performed. Results: In current study, association of ADAR1 with OV20.0 was evidenced for the first time. Consistently, C-terminal DRBD of OV20.0, and the first DRBD of ADAR1 are critical for this interaction. Furthermore, we found mCherry-tagged ADAR1 colocalized with two OV20.0 isoforms, the full length and N terminal truncated OV20.0 (sh20), in nucleus. Interestingly, ARAD1 was also shuttled to cytoplasm in the proximity of sh20 in a subset of cells that indicates the interaction between ADAR1 and sh20 possibly alters their cellular distribution. Conclusion: OV20.0 associates with cellular ADAR1 protein via their DRBD. Furthermore, among the three DRBDs, the first DRBD of ADAR1 is critical for their interaction. The consequence of interaction leads to re-distribution of ADAR1 to cytoplasm, indicating that OV20.0 possibly influences the function of ADAR1.
Appears in Collections:	[Department of Beauty Science] Papers

Files in This Item:

File	Description	Size	Format
林峰原IUMS2017-1713-v2 poster-ver2.0.pdf		14996Kb	Adobe PDF	0	View/Open

View Licence

Loading...