1887

Abstract

Most street rabies virus G proteins have two -glycosylation sites, i.e. Asn and Asn, whereas additional sites are found in fixed (laboratory adapted) viruses. In this study, we performed a pseudotyped virus assay using G-deficient rabies virus and demonstrated that single--glycan additions to the G protein of street rabies virus strain 1088, which are found in adapted strains, enhanced virus production in neural and non-neural cell lines, while additions to Asn or Asn enhanced production greatly. Moreover, we found that -glycan additions at Asn or Asn facilitated the production of cell-associated virus. In contrast, deletion of the sequon at Asn reduced viral production, while a deletion at Asn resulted in extensive loss of production. Furthermore, G proteins lacking an -glycan at Asn failed to fold into their correct structure and lost their fusion activity, indicating that Asn -glycosylation is important for the functional expression of street virus G proteins.

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2013-02-01
2021-10-28
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