scholarly journals Japanese Encephalitis Virus Replication and Inhibitory Effect of shRNA in Mice

2016 ◽  
Vol 06 (06) ◽  
pp. 462-470 ◽  
Author(s):  
Manabu Murakami ◽  
Takafumi Tasaki ◽  
Souichi Nukuzuma ◽  
Hiroshi Minato ◽  
Takayuki Nojima ◽  
...  
Keyword(s):  
Japanese Encephalitis Virus ◽  
Virus Replication ◽  
Japanese Encephalitis ◽  
Inhibitory Effect ◽  
Encephalitis Virus

Inhibitory effect of furanonaphthoquinone derivatives on the replication of Japanese encephalitis virus

1998 ◽  
Vol 37 (1) ◽  
pp. 37-45 ◽  
Author(s):  
Tsutomu Takegami ◽  
Eriko Simamura ◽  
Kei-Ichi Hirai ◽  
Junko Koyama
Keyword(s):  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Inhibitory Effect ◽  
Encephalitis Virus

Inhibitory Effect of RNAi on Japanese Encephalitis Virus ReplicationIn VitroandIn Vivo

2005 ◽  
Vol 49 (12) ◽  
pp. 1047-1056 ◽  
Author(s):  
Manabu Murakami ◽  
Takahide Ota ◽  
Soichi Nukuzuma ◽  
Tsutomu Takegami
Keyword(s):  
Japanese Encephalitis Virus ◽  
Japanese Encephalitis ◽  
Inhibitory Effect ◽  
Encephalitis Virus

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.

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