title: Proper maturation of the Japanese encephalitis virus envelope glycoprotein requires cosynthesis with the premembrane protein.
abstract: The role of the Japanese encephalitis virus (JEV) premembrane (prM) protein in maturation of the envelope (E) glycoprotein was evaluated by using recombinant vaccinia viruses encoding E in the presence (vP829) or absence (vP658) of prM. Immunofluorescence analyses showed that E appeared to be localized in the endoplasmic reticulum of cells infected with JEV, vP829, or vP658. However, reactivity with monoclonal antibodies and behavior in Triton X-114 indicated that E produced in the absence of prM behaved abnormally. Furthermore, E produced in the presence of prM by recombinant vaccinia viruses could be incorporated into flavivirus pseudotypes, whereas E synthesized in the absence of prM could not. These results demonstrate that cosynthesis of prM is required for proper folding, membrane association, and assembly of the flavivirus E protein.
authors.affiliation: Department of Medical Zoology, Kobe University School of Medicine, Japan.
authors.forename: E
authors.initials: E
authors.lastname: Konishi
authors.forename: P W
authors.initials: PW
authors.lastname: Mason
mesh_terms: D004664:Encephalitis Virus, Japanese / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D009500:Neutralization Tests; D011233:Precipitin Tests; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000378:metabolism; D014616:Vaccinia virus / Q000235:genetics; D014759:Viral Envelope Proteins / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D011498:Protein Precursors; D011994:Recombinant Proteins; D014759:Viral Envelope Proteins