Attenuated West Nile virus mutant NS1130-132QQA/175A/207A exhibits virus-induced ultrastructural changes and accumulation of protein in the endoplasmic reticulum

Melissa C. Whiteman; Vsevolod Popov; Michael B. Sherman; Julie Wen; Alan D.T. Barrett

doi:10.1128/JVI.02215-14

Attenuated West Nile virus mutant NS1_{130-132QQA/175A/207A} exhibits virus-induced ultrastructural changes and accumulation of protein in the endoplasmic reticulum

Melissa C. Whiteman, Vsevolod Popov, Michael B. Sherman, Julie Wen, Alan D.T. Barrett

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

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 NS1_{130-132QQA/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.

Original language	English (US)
Pages (from-to)	1474-1478
Number of pages	5
Journal	Journal of virology
Volume	89
Issue number	2
DOIs	https://doi.org/10.1128/JVI.02215-14
State	Published - 2015

ASJC Scopus subject areas

Microbiology
Immunology
Insect Science
Virology

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title = "Attenuated West Nile virus mutant NS1130-132QQA/175A/207A exhibits virus-induced ultrastructural changes and accumulation of protein in the endoplasmic reticulum",

abstract = "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.",

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AU - Popov, Vsevolod

AU - Sherman, Michael B.

AU - Wen, Julie

AU - Barrett, Alan D.T.

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AB - 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.

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Attenuated West Nile virus mutant NS1_{130-132QQA/175A/207A} exhibits virus-induced ultrastructural changes and accumulation of protein in the endoplasmic reticulum

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