A comparison of the pathogenesis of rabies virus SAD-L16 and mutants modified at the dynein light chain binding domain in the phosphoprotein and at position 333 in the glycoprotein in young mice

Recently the phosphoprotein of the rabies virus was shown to interact with the dynein light chain. This led to the speculation that perhaps dynein may be involved in the retrograde axonal transport of rabies virus in the nervous system. Intervet International deleted amino acids from the dynein binding domain on the phosphoprotein of rabies virus in an effort to impair axonal transport and create a new live attenuated rabies virus vaccine.; Two-day-old and seven-day-old ICR mice were inoculated either through the intracerebral or intramuscular route with SAD-L16, L-DeltaP11, D333 or D-DeltaP11. Mice were observed daily for clinical signs of rabies. Two to three mice from each virus group were sacrificed at serial time points and brains were examined to determine the rate of viral spread and histopathological changes caused by the viruses. Immunoperoxidase staining was used to detect rabies virus antigen and staining with cresyl violet and toluidine blue were used for histopathological examination. (Abstract shortened by UMI.)...