C19orf66 Inhibits Japanese Encephalitis Virus Replication by Targeting -1 PRF and the NS3 Protein

2021 ◽  
Author(s):  
Du Yu ◽  
Yundi Zhao ◽  
Junhui Pan ◽  
Xingmiao Yang ◽  
Zhenjie Liang ◽  
...  
Keyword(s):  
Japanese Encephalitis Virus ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Encephalitis Virus ◽  
Ns3 Protein

scholarly journals The DEAD-box RNA helicase DDX5 acts as a positive regulator of Japanese encephalitis virus replication by binding to viral 3′ UTR

2013 ◽  
Vol 100 (2) ◽  
pp. 487-499 ◽  
Author(s):  
Chen Li ◽  
Ling-ling Ge ◽  
Peng-peng Li ◽  
Yue Wang ◽  
Ming-xia Sun ◽  
...  
Keyword(s):  
Japanese Encephalitis Virus ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Rna Helicase ◽  
Encephalitis Virus ◽  
Positive Regulator ◽  
Dead Box ◽  
The Dead

scholarly journals ZBTB38 in Porcine Alveolar Macrophages Positively Regulates the Proliferation of Japanese Encephalitis Virus

2021 ◽  
Author(s):  
Yi Zheng ◽  
Yu-Yong Zhou ◽  
Chun-Xia Chai ◽  
San-Jie Cao ◽  
Qi-Gui Yan ◽  
...  
Keyword(s):  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Alveolar Macrophages ◽  
Encephalitis Virus ◽  
Porcine Alveolar Macrophage ◽  
Envelope Gene ◽  
Interacting Protein ◽  
Btb Domain ◽  
New Information ◽  
Ns3 Protein

Abstract Background Japanese encephalitis (JE) is an important zoonotic disease caused by Japanese encephalitis virus (JEV), and pigs are intermediate host of this disease. Previous studies have confirmed that JEV can proliferate in the respiratory tract of mice and spread through it. Therefore, this study aimed to screen the proteins interacting with JEV on porcine alveolar macrophage cell and verify its role in the proliferation of JEV.Methods and results Porcine alveolar macrophages cell line 3D4/21 were infected with JEV, and obvious cytopathic effect (CPE) was observed. Zinc finger and BTB domain containing 38 (ZBTB38) was screened out as an interacting protein using co-immunoprecipitation assay and validated through knockout and overexpression of ZBTB38 in 3D4/21 cells. The results demonstrated that loss of ZBTB38 function basically had no effect on the attachment and entry processes of JEV, while the transcription level of JEV envelope gene, the expression level of NS3 protein and the number of virions were all significantly down-regulated in the subsequent infection stage. Conclusion Overall, one core conclusion was drawn in this paper that ZBTB38 promotes the proliferation of JEV especially in the middle and late stages of infection. This study provides new information for understanding the pathogenic mechanism of JEV, especially the respiratory transmission caused by JEV infection.

scholarly journals Conserved amino acids 193–324 of non-structural protein 3 are a dominant source of peptide determinants for CD4+ and CD8+ T cells in a healthy Japanese encephalitis virus-endemic cohort

2004 ◽  
Vol 85 (5) ◽  
pp. 1131-1143 ◽  
Author(s):  
Priti Kumar ◽  
Paramadevanapalli Sulochana ◽  
Gejjehalli Nirmala ◽  
Maganti Haridattatreya ◽  
Vijaya Satchidanandam
Keyword(s):  
Amino Acids ◽  
T Cells ◽  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Cd8 T Cells ◽  
Encephalitis Virus ◽  
Structural Protein ◽  
Parent Protein ◽  
Ns3 Protein ◽  
Conserved Amino Acids

Our earlier identification of the non-structural protein 3 (NS3) of Japanese encephalitis virus (JEV) as a dominant CD4+ as well as CD8+ T cell-eliciting antigen in a healthy JEV-endemic cohort with a wide HLA distribution implied the presence of several epitopes dispersed over the length of the protein. Use of various truncated versions of NS3 in lymphocyte stimulation and interferon (IFN)-γ secretion assays revealed that amino acids (aa) 193–324 of NS3 were comparable with, if not superior to, the full-length protein in evoking Th1 responses. The potential of this 14·4 kDa stretch to stimulate IFN-γ production from both subtypes of T cells in a manner qualitatively and quantitatively similar to the 68 kDa parent protein suggested the presence within it of both class I and II epitopes and demonstrated that the entire immunogenicity of NS3 was focused on aa 193–324. Interestingly, this segment contained five of the eight helicase motifs of NS3. Analysis of variability of the NS3 protein sequence across 16 JEV isolates revealed complete identity of aa 219–318, which is contained within the above segment, suggesting that NS3-specific epitopes tend to cluster in relatively conserved regions that harbour functionally critical domains of the protein.

Porcine 2′, 5′-oligoadenylate synthetases inhibit Japanese encephalitis virus replication in vitro

2015 ◽  
Vol 88 (5) ◽  
pp. 760-768 ◽  
Author(s):  
Sheng Zheng ◽  
Dan Zhu ◽  
Xue Lian ◽  
Weiting Liu ◽  
Ruibing Cao ◽  
...  
Keyword(s):  
Japanese Encephalitis Virus ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Encephalitis Virus

scholarly journals Japanese encephalitis virus capsid protein interacts with non-lipidated MAP1LC3 on replication membranes and lipid droplets

2020 ◽  
Author(s):  
Riya Sarkar ◽  
Kiran Bala Sharma ◽  
Anita Kumari ◽  
Shailendra Asthana ◽  
Manjula Kalia
Keyword(s):  
Japanese Encephalitis Virus ◽  
Capsid Protein ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Lipid Droplets ◽  
Adaptor Protein ◽  
Protein Docking ◽  
Encephalitis Virus ◽  
Virus Capsid ◽  
Virus Capsid Protein

Microtubule-associated protein 1 light chain 3 (MAP1LC3) is a protein with a well-defined function in autophagy, but still incompletely understood roles in several other autophagy-independent processess. Studies have shown MAP1LC3 is a host-dependency factor for the replication of several viruses. Japanese encephalitis virus (JEV), a neurotropic flavivirus, replicates on ER-derived membranes that are marked by autophagosome-negative non-lipidated MAP1LC3 (LC3-I). Depletion of LC3 exerts a profound inhibition on virus replication and egress. Here, we further characterize the role of LC3 in JEV replication, and through immunofluorescence and immunoprecipitation show that LC3-I interacts with the virus capsid protein in infected cells. This association was observed on capsid localized to both the replication complex and lipid droplets (LDs). JEV infection decreased the number of LDs per cell indicating a link between lipid metabolism and virus replication. This capsid-LC3 interaction was independent of the autophagy adaptor protein p62/Sequestosome 1 (SQSTM1). Further, no association of capsid was seen with the Gamma-aminobutyric acid receptor-associated protein family, suggesting that this interaction was specific for LC3. High-resolution protein-protein docking studies identified a putative LC3-interacting region in capsid, 56FTAL59, and other key residues that could mediate a direct interaction between the two proteins.

scholarly journals Japanese encephalitis virus capsid protein interacts with non-lipidated MAP1LC3 on replication membranes and lipid droplets

2020 ◽  
Author(s):  
Riya Sarkar ◽  
Kiran Bala Sharma ◽  
Anita Kumari ◽  
Shailendra Asthana ◽  
Manjula Kalia
Keyword(s):  
Japanese Encephalitis Virus ◽  
Capsid Protein ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Lipid Droplets ◽  
Adaptor Protein ◽  
Protein Docking ◽  
Encephalitis Virus ◽  
Virus Capsid ◽  
Virus Capsid Protein

AbstractStudies have shown that Japanese encephalitis virus (JEV), replicates on ER derived membranes that are marked by autophagosome negative non-lipidated MAP1LC3 (LC3-I). Depletion of LC3 exerts a profound inhibition on virus replication and egress. Here, we further characterize the role of LC3 in JEV replication, and through immunofluorescence and immunoprecipitation show that LC3-I interacts with the virus capsid protein in infected cells. This association was observed on capsid localized to both the replication complex and lipid droplets (LDs). JEV infection decreased the number of LDs per cell indicating a link between lipid metabolism and virus replication. This capsid-LC3 interaction was independent of the autophagy adaptor protein p62/SQSTM1. Further, no association of capsid was seen with the GABARAP protein family, suggesting that this interaction was specific for LC3. High resolution protein-protein docking studies identified a putative LC3-interacting region (LIR) in capsid, 56FTAL59, and other key residues that could mediate a direct interaction between the two proteins.

scholarly journals Artificial MicroRNA-Mediated Inhibition of Japanese Encephalitis Virus Replication in Neuronal Cells

2018 ◽  
Vol 28 (6) ◽  
pp. 357-365 ◽  
Author(s):  
Himani Sharma ◽  
Aarti Tripathi ◽  
Bharti Kumari ◽  
Sudhanshu Vrati ◽  
Arup Banerjee
Keyword(s):  
Japanese Encephalitis Virus ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Neuronal Cells ◽  
Encephalitis Virus ◽  
Artificial Microrna
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