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Rabies virus surface glycoprotein (rabies G-protein) with (G+RS) and without (G−RS) endoplasmic reticulum retrieval signal was expressed and characterized in tobacco plants. Transgenically expressed rabies G-protein was estimated at 0.015–0.38 % of total leaf protein. The relative migration of the rabies G-protein on SDS-PAGE was at the position, as anticipated for the viral coat protein (~66 kDa). Immunolocalization by confocal microscopy established that immunoprotective G+RS expressed in tobacco was primarily confined to ER. G+RS showed binding to Con A lectin and was susceptible to N-glycosidase F activity similar to native rabies G-protein. However, the G−RS transgenically expressed in tobacco leaves was glycosylated differently and was resitant to N-glycosidase F. Immunological studies and Rapid Fluorescent Foci Inhibition Test (RFFIT) showed that G+RS was immunogenic and …