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Four well-characterized monoclonal antibodies (MAbs) directed against rabies virus glycoprotein (G) were used to study G folding in vivo. Two of the MAbs were able to immunoprecipitate incompletely oxidized folding intermediates. The two others recognized G only after folding was completed. By using these MAbs, the ability of G to undergo low-pH-induced conformational changes during folding was also investigated. It appeared that some domains acquire this ability before folding is completed. In addition, interactions between unfolded G and some of the molecular chaperones were analyzed. Unfolded G was associated with BiP and calnexin. Association with BiP was maximal immediately after the pulse, whereas association with calnexin was maximal after 5 to 10 min of chase. The effects of tunicamycin and castanospermine on chaperone binding and folding were also studied. In the presence of both drugs, calnexin binding was reduced, consistent with the view that calnexin specifically recognizes monoglucosylated oligosaccharides, but some residual binding was still observed, indicating that calnexin also recognizes the polypeptide chain. In the presence of both drugs, association with BiP was increased and prolonged and folding was impaired. However, the global effects of the drugs were different, since folding was much more efficient in the presence of castanospermine than in the presence of tunicamycin. Taken together, these results provide the basis to draw a schematic view of rabies virus glycoprotein folding.

Folding of rabies virus glycoprotein: epitope acquisition and interaction with endoplasmic reticulum chaperones