scholarly journals BST2 suppresses porcine epidemic diarrhea virus replication by targeting and degrading virus nucleocapsid protein with selective autophagy

Autophagy ◽  
2019 ◽  
Vol 16 (10) ◽  
pp. 1737-1752 ◽  
Author(s):  
Ning Kong ◽  
Tongling Shan ◽  
Hua Wang ◽  
Yajuan Jiao ◽  
Yewen Zuo ◽  
...  
Keyword(s):  
Virus Replication ◽  
Porcine Epidemic Diarrhea Virus ◽  
Nucleocapsid Protein ◽  
Diarrhea Virus ◽  
Selective Autophagy ◽  
Porcine Epidemic Diarrhea

scholarly journals Molecular Characterizations of Subcellular Localization Signals in the Nucleocapsid Protein of Porcine Epidemic Diarrhea Virus

Viruses ◽  
2014 ◽  
Vol 6 (3) ◽  
pp. 1253-1273 ◽  
Author(s):  
Da Shi ◽  
Maojie Lv ◽  
Jianfei Chen ◽  
Hongyan Shi ◽  
Sha Zhang ◽  
...  
Keyword(s):  
Subcellular Localization ◽  
Porcine Epidemic Diarrhea Virus ◽  
Nucleocapsid Protein ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

scholarly journals Cellular hnRNP A1 Interacts with Nucleocapsid Protein of Porcine Epidemic Diarrhea Virus and Impairs Viral Replication

Viruses ◽  
2018 ◽  
Vol 10 (3) ◽  
pp. 127 ◽  
Author(s):  
Zhonghua Li ◽  
Wei Zeng ◽  
Shiyi Ye ◽  
Jian Lv ◽  
Axiu Nie ◽  
...  
Keyword(s):  
Viral Replication ◽  
Porcine Epidemic Diarrhea Virus ◽  
Nucleocapsid Protein ◽  
Hnrnp A1 ◽  
Diarrhea Virus ◽  
Porcine Epidemic Diarrhea

scholarly journals Porcine Epidemic Diarrhea Virus (PEDV) ORF3 Interactome Reveals Inhibition of Virus Replication by Cellular VPS36 Protein

Viruses ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 382 ◽  
Author(s):  
Challika Kaewborisuth ◽  
Yodying Yingchutrakul ◽  
Sittiruk Roytrakul ◽  
Anan Jongkaewwattana
Keyword(s):  
Virus Replication ◽  
Porcine Epidemic Diarrhea Virus ◽  
Interacting Proteins ◽  
Gene Ontology Analysis ◽  
Orf3 Gene ◽  
Orf3 Protein ◽  
Diarrhea Virus ◽  
Host Interaction ◽  
Porcine Epidemic Diarrhea ◽  
Vacuolar Protein

The accessory protein ORF3 of porcine epidemic diarrhea virus (PEDV) has been proposed to play a key role in virus replication. However, our understanding of its function regarding virus and host interaction is still limited. In this study, we employed immunoprecipitation and mass spectrometry to screen for cellular interacting partners of ORF3. Gene ontology analysis of the host interactome highlighted the involvement of ORF3 in endosomal and immune signaling pathways. Among the identified ORF3-interacting proteins, the vacuolar protein-sorting-associated protein 36 (VPS36) was assessed for its role in PEDV replication. VPS36 was found to interact with ORF3 regardless of its GLUE domain. As a result of VPS36–ORF3 interaction, PEDV replication was substantially suppressed in cells overexpressing VPS36. Interestingly, the ORF3 protein expression was diminished in VPS36-overexpressing cells, an effect that could not be restored by treatment of lysosomal inhibitors. In addition, disruption of endogenously-expressed VPS36 by siRNA could partially augment PEDV replication. Taken together, our study provides mechanistic insights into the contribution of ORF3 in PEDV replication.

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