Summary. -Premembrane (prM) and envelope (E) proteins, the major structural proteins of Japanese encephalitis virus (JEV) each contain single potential N-glycosylation site. In this study, the role of N-glycosylation of these proteins on their folding and activity were investigated. Three mutant prM and/or E (prM-E) genes lacking N-glycosylation sites were generated by site-directed mutagenesis. The effects of the N-glycan on folding, secretion and cytotoxicity of mutant proteins were determined by comparison with their wild type (wt) counterparts. Removal of N-glycan from the prM protein resulted in a complete misfolding of the E protein and failure to form virus-like particles (VLPs). A similar removal of N-glycan from the E protein led to a low efficiency of its folding and VLPs formation. The secretion and cytotoxicity of the E protein was also markedly impaired in case the glycosylation sites in the prM or E or both proteins were removed. These results suggest that the N-glycosylation of the prM protein is critical to the folding of the E protein, which makes it pivotal in the cytotoxicity of JEV particles and their production.Keywords: Japanese encephalitis virus; premembrane protein; envelope protein; N-glycosylation; protein folding; virus-like particles; secretion; cytotoxicity * Corresponding author. E-mail: syf@mail.hzau.edu.cn; phone: +86-27-87618028. Abbreviations: CE = conformational epitope; E = envelope; ER = endocytoplasmic reticulum; JEV = Japanese encephalitis virus; LE = linear epitope; MAb(s) = monoclonal antibody(ies) prM = premembrane; VLPs = virus-like particles
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