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- W3171975529 abstract "Flaviviruses is a genus within the family Flaviviridae. The genus consists of morethan 70 viruses, including important threatening human pathogens such as denguevirus (DENV), West Nile virus (WNV), and Zika virus (ZIKV). These viruses arecausative agents for a range of mild to lethal diseases and there are currently no US-licensed therapeutic treatments for infection. The virus genome is a positive-sense,single-stranded RNA, encoding ten viral proteins. Of the ten flavivirus proteins, Non-Structural protein 1 (NS1) remains the most elusive in terms of its functions. To dateNS1 has been linked to disease pathology and progression and plays roles in virusreplication and assembly. However, little is understood how NS1 orchestrates thesefunctions and how NS1 from different viruses function distinctively from one another.Moreover, flavivirus NS1 has a peculiar ability to associate with lipid membranes.During the life cycle of NS1, the protein travels through the classical secretory path-way, similar to infectious virus particles, and is secreted into the extracellular space asmostly hexameric oligomers containing a lipid core. How the protein binds to lipidsand whether such lipid binding is important for NS1 functions and overall flaviviruspathology remain unknown. Using structure-based mutagenesis, we found a groupof mutants on WNV NS1, which particularly altered the viral specific infectivitybut maintained wild-type level of virus replication. Purified mutated virus particlesrevealed that the specific infectivity alteration was not because of the particle butinteraction of the virus particles and NS1 mutated proteins. Here we demonstratedthat specific residues on NS1 were responsible for distinctly roles in NS1 functions andthe virus specific infectivity was regulated by NS1 protein. In other structure-base study, we focused on the membrane association ability of NS1. All structure-predictedregions on NS1 were examined for its contribution for the membrane/lipid bindingfunction. This interaction was required for NS1 biology activities including intracel-lular trafficking, oligomerization, and endocytosis. The lipidomes from deletion ofeach membrane association region revealed differences in lipid classes binding to eachregion and the composition flexiblity of the lipid cargo of NS1 hexamer." @default.
- W3171975529 created "2021-06-22" @default.
- W3171975529 creator A5012320915 @default.
- W3171975529 date "2020-04-17" @default.
- W3171975529 modified "2023-09-23" @default.
- W3171975529 title "Structure- Function Studies Of Flavivirus Non-Structural Protein1" @default.
- W3171975529 doi "https://doi.org/10.25394/pgs.12111486.v1" @default.
- W3171975529 hasPublicationYear "2020" @default.
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