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The Japanese encephalitis virus (JEV) structural proteins other than the envelope (E) protein consist of the capsid (C) and the pre-membrane (prM) proteins. The C protein is a small, highly basic protein that binds to the viral RNA genome to form the nucleocapsid, which is essential for viral assembly and the protection of the viral genome (Source 1.2.4, 1.4.2). It also interacts with host factors such as lipid droplets and the autophagy-related protein LC3-I to facilitate viral replication and pathogenesis (Source 1.4.3). The prM protein acts as a chaperone for the E protein, ensuring its proper folding and preventing premature fusion within the acidic environment of the host's secretory pathway (Source 1.2.2, 1.3.3). During the maturation of the virus, prM is cleaved by the host protease furin into the membrane (M) protein and a "pr" peptide, which is released upon virion exit (Source 1.1.1, 1.2.1). Both C and prM are considered potential therapeutic targets; research has explored inhibitors of nucleocapsid assembly (such as ST-148 analogs) and maturation processes (such as furin inhibitors) to block JEV infection (Source 1.2.4, 1.4.1).
Inhibition of nucleocapsid assembly by targeting the C protein and prevention of viral maturation by inhibiting prM cleavage.
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