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

Microtubule-associated protein 1 light chain 3 (MAP1LC3) is a with well-defined function in autophagy, but still incompletely understood roles several other autophagy-independent processess. Studies have shown MAP1LC3 host-dependency factor for the replication of viruses. Japanese encephalitis virus (JEV), neurotropic flavivirus, replicates on ER-derived membranes that are marked by autophagosome-negative non-lipidated (LC3-I). Depletion LC3 exerts profound inhibition and egress. Here, we further characterize role JEV replication, through immunofluorescence immunoprecipitation show LC3-I interacts capsid infected cells. This association was observed localized to both complex lipid droplets (LDs). infection decreased number LDs per cell indicating link between metabolism replication. capsid-LC3 interaction independent autophagy adaptor p62/Sequestosome (SQSTM1). Further, no seen Gamma-aminobutyric acid receptor-associated family, suggesting this specific LC3. High-resolution protein-protein docking studies identified putative LC3-interacting region capsid, 56 FTAL 59 , key residues could mediate direct two proteins.