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• W2095015093 startingPage "96" @default.
• W2095015093 abstract "West Nile virus (WNV) is a mosquito-transmitted pathogen, which causes significant disease in humans. The innate immune system is a first-line defense against invading microorganism and many flaviviruses, including WNV, have evolved multifunctional proteins, which actively suppress its activation and antiviral actions. The WNV non-structural protein 1 (NS1) inhibits signal transduction originating from Toll-like receptor 3 (TLR3) and also critically contributes to virus genome replication. In this study we developed a novel FACS-based screen to attempt to separate these two functions. The individual amino acid changes P320S and M333V in NS1 restored TLR3 signaling in virus-infected HeLa cells. However, virus replication was also attenuated, suggesting that the two functions are not easily separated and may be contained within overlapping domains. The residues we identified are completely conserved among several mosquito- and tick-borne flaviviruses, indicating that they are of biological importance to the virus." @default.
• W2095015093 created "2016-06-24" @default.
• W2095015093 creator A5040888638 @default.
• W2095015093 creator A5057080078 @default.
• W2095015093 date "2014-05-01" @default.
• W2095015093 modified "2023-10-18" @default.
• W2095015093 title "Abrogation of TLR3 inhibition by discrete amino acid changes in the C-terminal half of the West Nile virus NS1 protein" @default.
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• W2095015093 doi "https://doi.org/10.1016/j.virol.2014.03.017" @default.
• W2095015093 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4044628" @default.
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