Most street rabies virus glycoproteins (G proteins) possess two N -glycosylation sites, at Asn 37 and Asn 319 , whereas an additional N -glycosylation site is present in several fixed (laboratory-adapted) rabies virus strains at Asn 247 , which suggests that the N -glycosylation addition may be a marker of fixed viruses. In this study, we successfully cloned two street virus strain 1088 variants, N5B#15 and N5B#10-28, in which the G proteins had an additional N -glycan at position 247, and we examined whether these variants were characterized by cell culture adaptation and attenuation after intramuscular inoculation as fixed viruses. N5B#15 had four mutations, i.e., S148P and D247N in the G protein, and T137A and N2046S in the large (L) protein. N5B#10-28 had an additional mutation in the G protein, R196I. Compared with the parental 1088 virus, both variants exhibited highly efficient replication in mouse neuroblastoma-derived NA cells and reduced pathogenicity in adult mice when inoculated intramuscularly, but not intracerebrally. However, this attenuation was not attributable to the induction of strong immune responses.
Archives of Virology – Springer Journals
Published: Feb 1, 2014
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