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We have previously shown that ablation of the three N-linked glycosylation sites in the West Nile virus NS1 protein completely attenuates mouse neuroinvasiveness (≥1,000,000 PFU). Here, we compared the replication of the NS1130-132QQA/175A/207A mutant to that of the parental NY99 strain in monkey kidney Vero cells. The results suggest that the mechanism of attenuation is a lack of NS1 glycosylation, which blocks efficient replication, maturation, and NS1 secretion from the endoplasmic reticulum and results in changes to the virus-induced ultrastructure.

journal of virology

Attenuated West Nile Virus Mutant NS1 <sub>130-132QQA/175A/207A</sub> Exhibits Virus-Induced Ultrastructural Changes and Accumulation of Protein in the Endoplasmic Reticulum

Attenuated West Nile Virus Mutant NS1 130-132QQA/175A/207A Exhibits Virus-Induced Ultrastructural Changes and Accumulation of Protein in the Endoplasmic Reticulum

Attenuated West Nile Virus Mutant NS1 _{130-132QQA/175A/207A} Exhibits Virus-Induced Ultrastructural Changes and Accumulation of Protein in the Endoplasmic Reticulum