Characterization of street rabies virus variants with an additional N -glycan at position 247 in the glycoprotein

Characterization of street rabies virus variants with an additional N -glycan at position 247 in... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Archives of Virology Springer Journals

Characterization of street rabies virus variants with an additional N -glycan at position 247 in the glycoprotein

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Publisher
Springer Vienna
Copyright
Copyright © 2014 by Springer-Verlag Wien
Subject
Biomedicine; Virology; Medical Microbiology; Infectious Diseases
ISSN
0304-8608
eISSN
1432-8798
D.O.I.
10.1007/s00705-013-1805-5
Publisher site
See Article on Publisher Site

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