scholarly journals West Nile virus and dengue virus capsid protein negates the antiviral activity of human Sec3 protein through the proteasome pathway

2013 ◽  
pp. n/a-n/a ◽  
Author(s):  
Raghavan Bhuvanakantham ◽  
Mah-Lee Ng
Keyword(s):  
West Nile Virus ◽  
Antiviral Activity ◽  
Dengue Virus ◽  
Capsid Protein ◽  
West Nile ◽  
Virus Capsid ◽  
Proteasome Pathway ◽  
Virus Capsid Protein

scholarly journals Interactions between the West Nile virus capsid protein and the host cell-encoded phosphatase inhibitor, I2PP2A

2007 ◽  
Vol 9 (11) ◽  
pp. 2756-2766 ◽  
Author(s):  
Tracey A. Hunt ◽  
Matthew D. Urbanowski ◽  
Kishore Kakani ◽  
Lok-Man J. Law ◽  
Margo A. Brinton ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Host Cell ◽  
Capsid Protein ◽  
The West ◽  
West Nile ◽  
Virus Capsid ◽  
Phosphatase Inhibitor ◽  
Virus Capsid Protein

scholarly journals Jab1 Mediates Cytoplasmic Localization and Degradation of West Nile Virus Capsid Protein

2006 ◽  
Vol 281 (40) ◽  
pp. 30166-30174 ◽  
Author(s):  
Wonkyung Oh ◽  
Mi-Ran Yang ◽  
Eun-Woo Lee ◽  
Ki-moon Park ◽  
Suhkneung Pyo ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Capsid Protein ◽  
Cytoplasmic Localization ◽  
West Nile ◽  
Virus Capsid ◽  
Virus Capsid Protein

scholarly journals MKRN1 Induces Degradation of West Nile Virus Capsid Protein by Functioning as an E3 Ligase

2009 ◽  
Vol 84 (1) ◽  
pp. 426-436 ◽  
Author(s):  
Aram Ko ◽  
Eun-Woo Lee ◽  
Jung-Yong Yeh ◽  
Mi-Ran Yang ◽  
Wonkyung Oh ◽  
...  
Keyword(s):  
Amino Acids ◽  
West Nile Virus ◽  
Capsid Protein ◽  
Ring Finger ◽  
Dependent Manner ◽  
West Nile ◽  
Apoptotic Pathway ◽  
Cytotoxic Effects ◽  
Virus Capsid ◽  
Virus Capsid Protein

ABSTRACT West Nile virus capsid protein (WNVCp) displays pathogenic toxicity via the apoptotic pathway. However, a cellular mechanism protective against this toxic effect has not been observed so far. Here, we identified Makorin ring finger protein 1 (MKRN1) as a novel E3 ubiquitin ligase for WNVCp. The cytotoxic effects of WNVCp as well as its expression levels were inhibited in U2OS cells that stably expressed MKRN1. Immunoprecipitation analyses revealed an interaction between MKRN1 and WNVCp. Domain analysis indicated that the C terminus of MKRN1 and the N terminus of WNVCp were required for the interaction. MKRN1 could induce WNVCp ubiquitination and degradation in a proteasome-dependent manner. Interestingly, the WNVCp mutant with amino acids 1 to 105 deleted WNVCp was degraded by MKRN1, whereas the mutant with amino acids 1 to 90 deleted was not. When three lysine sites at positions 101, 103, and 104 of WNVCp were replaced with alanine, MKRN1-mediated ubiquitination and degradation of the mutant were significantly inhibited, suggesting that these sites are required for the ubiquitination. Finally, U2OS cell lines stably expressing MKRN1 were resistant to cytotoxic effects of WNV. In contrast, cells depleted of MKRN1 were more susceptible to WNVCp cytotoxicity. Confirming this, overexpression of MKRN1 significantly reduced, but depletion of MKRN1 increased, WNV proliferation in 293T cells. Taken together, our results suggest that MKRN1 can protect cells from WNV by inducing WNVCp degradation.

scholarly journals West Nile virus capsid protein inhibits autophagy by AMP-activated protein kinase degradation in neurological disease development

2020 ◽  
Vol 16 (1) ◽  
pp. e1008238 ◽  
Author(s):  
Shintaro Kobayashi ◽  
Kentaro Yoshii ◽  
Wallaya Phongphaew ◽  
Memi Muto ◽  
Minato Hirano ◽  
...  
Keyword(s):  
West Nile Virus ◽  
Protein Kinase ◽  
Capsid Protein ◽  
Neurological Disease ◽  
Disease Development ◽  
West Nile ◽  
Virus Capsid ◽  
Amp Activated Protein Kinase ◽  
Virus Capsid Protein

scholarly journals West Nile Virus Capsid Protein Interacts With Biologically Relevant Host Lipid Systems

2019 ◽  
Vol 9 ◽  
Author(s):  
Ana S. Martins ◽  
Filomena A. Carvalho ◽  
André F. Faustino ◽  
Ivo C. Martins ◽  
Nuno C. Santos
Keyword(s):  
West Nile Virus ◽  
Capsid Protein ◽  
West Nile ◽  
Virus Capsid ◽  
Biologically Relevant ◽  
Virus Capsid Protein
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