C-terminal 20 residues of ORF3 protein of duck circovirus genotype 2 regulates the nuclear localization and inhibits apoptotic activity of ORF3 protein

2018 ◽  
Vol 214 ◽  
pp. 21-27 ◽  
Author(s):  
Zhuan-Chang Wu ◽  
Rui-Hua Zhang ◽  
Yu-Ming Li ◽  
Dong-Hua Shao ◽  
Hua Chen ◽  
...  
Author(s):  
Yanting Zhang ◽  
Xingcui Zhang ◽  
Anchun Cheng ◽  
Mingshu Wang ◽  
Zhongqiong Yin ◽  
...  

Apoptosis, a form of the programmed cell death, is an indispensable defense mechanism regulating cellular homeostasis and is triggered by multiple stimuli. Because of the regulation of apoptosis in cellular homeostasis, viral proteins with apoptotic activity are particular foci of on antitumor therapy. One representative viral protein is the open reading frame 3 (ORF3) protein, also named as apoptin in the Circoviridae chicken anemia virus (CAV), and has the ability to induce tumor-specific apoptosis. Proteins encoded by ORF3 in other circovirus species, such as porcine circovirus (PCV) and duck circovirus (DuCV), have also been reported to induce apoptosis, with subtle differences in apoptotic activity based on cell types. This article is aimed at reviewing the latest research advancements in understanding ORF3 protein-mediated apoptosis mechanisms of Circoviridae from three perspectives: subcellular localization, interactions with host proteins, and participation in multiple apoptotic signaling pathways, providing a scientific basis for circovirus pathogenesis and a reference on its potential anticancer function.


2007 ◽  
Vol 354 (2) ◽  
pp. 391-395 ◽  
Author(s):  
Yen-Hsien Lee ◽  
Chih-Mei Cheng ◽  
Yung-Fu Chang ◽  
Ting-Yi Wang ◽  
Chung-Yee Yuo

2004 ◽  
Vol 85 (5) ◽  
pp. 1329-1333 ◽  
Author(s):  
Eugene V. Ryabov ◽  
Sang Hyon Kim ◽  
Michael Taliansky

The 27 kDa protein encoded by ORF3 of Groundnut rosette virus (GRV) is required for viral RNA protection and movement of viral RNA through the phloem. Localization studies have revealed that this protein is located in nuclei, preferentially targeting nucleoli. We have demonstrated that amino acids (aa) 108–122 of the GRV ORF3 protein contain an arginine-rich nuclear localization signal. Arginine-to-asparagine substitutions in this region decreased the level of the ORF3 protein accumulation in nuclei. A leucine-rich nuclear export signal (NES) was located at aa 148–156 of the GRV ORF3 protein. Leucine-to-alanine substitutions in this region resulted in a dramatic increase in GRV ORF3 protein accumulation in both nuclei and nucleoli. Consistent with this, we also showed that the previously identified NES of BR1 protein of Squash leaf curl virus can functionally replace the leucine-rich region of GRV ORF3 in nuclear export.


Virology ◽  
2013 ◽  
Vol 436 (1) ◽  
pp. 112-117 ◽  
Author(s):  
Qi-Wang Xiang ◽  
Jin-Feng Zou ◽  
Xin Wang ◽  
Ya-Ni Sun ◽  
Ji-Ming Gao ◽  
...  

2015 ◽  
Vol 59 (04) ◽  
pp. 423-428
Author(s):  
X. WANG ◽  
Z. WU ◽  
Q. XIANG ◽  
Z. LI ◽  
R. ZHANG ◽  
...  

2012 ◽  
Vol 159 (1-2) ◽  
pp. 251-256 ◽  
Author(s):  
Qi-Wang Xiang ◽  
Xin Wang ◽  
Zhi-Jing Xie ◽  
Ya-Ni Sun ◽  
Yan-Li Zhu ◽  
...  

2005 ◽  
Vol 173 (4S) ◽  
pp. 105-106
Author(s):  
Ismaël H. Koumakpayi ◽  
Jean-Simon Diallo ◽  
Cecile Le Page ◽  
Laurent Lessard ◽  
Martin E. Gleave ◽  
...  

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