literature

IV mutation literature information.

Adsorptive mutation and N-linked glycosylation modulate influenza virus antigenicity and fitness.

PMID: 33179567 2020 Emerging microbes & infections

Discussion: First, growing wild type SKP-827/16 virus that naturally contains T180 led to the addition of HA D189N which glycosylated residue 189, indicating proven biological relevance to studying N-linked glycans.

Altering Intracellular Localization of the RNA Interference Factors by Influenza A Virus Non-structural Protein 1.

PMID: 33281788 2020 Frontiers in microbiology

Method: Individual point mutations were introduced into the NS segment of PR8 (D101H, A155T, and D189N of PR8 NS1 protein, see below) and the mutant viruses rescued by standard procedures using an eight-plasmid reverse genetics system.

Result: Cell fractionation analysis showed that similar to IAV-PR8, infection with neither PR8-NS1 (A155T) nor PR8-NS1 (D189N) enhanced nuclear accumulation of AGO2 (Figure 4A lane 4,5).

Result: Furthermore, we found that endogenous miR-16 accumulated to much higher levels in the nucleus of 293T cells following infection with PR8 7 + 1 or PR8-NS1 (D101H), but not

Identification of two residues within the NS1 of H7N9 influenza A virus that critically affect the protein stability and function.

PMID: 30285871 2018 Veterinary research

Introduction: I64T, D189N and V194I mutations in NS1 protein of circulating H3N2 human influenza virus weakened NS1-mediated general inhibition of host protein synthesis by decreasing its interaction with cleavage and polyadenylation specificity factor 30 (CPSF30), leading to attenuated virulence and increased innate immune responses after the viral infection.

NS1 Protein Amino Acid Changes D189N and V194I Affect Interferon Responses, Thermosensitivity, and Virulence of Circulating H3N2 Human Influenza A Viruses.

PMID: 28003482 2017 Journal of virology

Abstract: NS1 mutations D189N and V194I impaired the ability of the NS1 protein to inhibit general gene expression, and recombinant viruses harboring these mutations were attenuated in a mouse model of influenza infection.

Abstract: A recombinant A/Puerto Rico/8/34 (PR8) H1N1 virus encoding the H3N2 NS1-D189N protein was slightly attenuated, whereas the virus encoding the H3N2 NS1-V194I protein was further attenuated in mice.

Abstract: The consequences of these mutations for the NS1-mediated inhibition of IFN responses and the pathogenesis of the virus were evaluated, showing that NS1

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