Risk of Environmental Exposure to H7N9 Influenza Virus via Airborne and Surface Routes in a Live Poultry Market in Hebei, China.
PMID: 34164347
2021
Frontiers in cellular and infection microbiology
Introduction: reported that mutations in PB2 (E627K), NA (R294K) and PA (V100A) were significantly correlated with increased mortality, while other mutations in HA (N276D) and PB2 (N559T) were distinctly correlated with mild cases.
A study of the relationship between human infection with avian influenza a (H5N6) and environmental avian influenza viruses in Fujian, China.
Abstract: The R294K or N294S substitution was not detected in the neuraminidase (NA).
Result: Neither R294K nor N294S substitution was detected in the NA genes of all the eight H5N6 viruses, indicating a general sensitivity to Oseltamivir and Zanamivir antiviral drugs.
Table: R294K
Antiviral Activity of Benzoic Acid Derivative NC-5 Against Influenza A Virus and Its Neuraminidase Inhibition.
PMID: 31842256
2019
International journal of molecular sciences
Met
Method: Plasmid construction: The recombinant plasmids pcDNA3.1(+), which can stably express NA protein sequences of A/Vietnam/1203/2004 (H5N1), A/Anhui/1/2013 (H7N9) and A/Anhui/1/2013-R294K (H7N9-R294K) were transfected into CHO-K1 cells using Lipofectamine 2000 Reagent (Invitrogen , Carlsbad, CA, USA).
Result: NC-5 suppressed the NA activity of H1N1-H275Y and H7N9-R294K and the inhibition rates were both 25.8% at 480 muM.
Result: The NA activities of oseltamivir-resistant viruses H1N1-H275Y (Figure 2A) and H7N9-R294K (Figure 2C) were also inhibited by NC-5 with a weaker or similar inhibition effect.
Table: R294K
The inhibitory effect of sodium baicalin on oseltamivir-resistant influenza A virus via reduction of neuraminidase activity.
PMID: 29572682
2018
Archives of pharmacal research
Abstract: Direct interactions between sodium baicalin and NA were observed, and we simulated the interactions of sodium baicalin with N9-R294K and N9 near the active sites of OC-N9-R294K and OC-N9.
Abstract: The IC50 values of sodium baicalin against H1N1-H275Y and cells-expressing A/Anhui/1/2013-R294K (H7N9-R294K) NA protein (N9-R294K) were 214.4 muM and 216.3 muM.
Abstract: The residues responsible for the sodium baicalin-N9-R294K and sodium baicalin-
[Genetic characteristics of hemagglutinin and neuraminidase of avian influenza A (H7N9) virus in Guizhou province, 2014-2017].
PMID: 30462955
2018
Zhonghua liu xing bing xue za zhi
1Abstract: All the strains had a stalk deletion of 5 amino acid residue ""QISNT"" in NA protein, and drug resistance mutation R294K occurred in strain A/Guizhou-Danzhai/18980/2017."
Identification of novel compounds against an R294K substitution of influenza A (H7N9) virus using ensemble based drug virtual screening.
PMID: 25589893
2015
International journal of medical sciences
Conclusion: In this study, we demonstrated resistant mechanism of mutant strain H7N9 (R294K) in Shanghai virus by comparing binding poses and binding affinity between inhibitors as well as the substrate and X-ray structure of mutant and wild type NA in H7N9 virus.
Conclusion: Therefore, we concluded that 7181 is the best potential compound for NA (R294K) inhibition and should be further analyzed and served as drug candidate for in vivo testing.
Introduction: Unexpectedly, all novel influenza A H7N9 viruses possess the mutation S31N in
Result: These results explain experimental data that R294K substitution led to extreme resistance of NA to Oseltamivir and conferred less resistance to Peramivir, Zanamivir and Laninarmivir.
Molecular docking of potential inhibitors for influenza H7N9.
PMID: 25861376
2015
Computational and mathematical methods in medicine
Abstract: Further analyses showed that R294K mutation in neuraminidase could remarkably decrease the binding energies for oseltamivir, while other small molecules showed stable binding abilities with mutated neuraminidase.
Introduction: Furthermore, the authors proposed that the drug resistance caused by mutation of R294K in H7N9 was more serious than that caused by mutation of H274Y in H7N1.
Introduction: solved the structures for neuraminidases of A/Anhui/1/2013 (Result: These results indicated that the oseltamivir resistance caused by R294K mutation for neuraminidase in A/Shanghai/1/2013 might be generated from the H-bond loss, while other molecules might overcome the resistance.
A novel pyrosequencing assay for the detection of neuraminidase inhibitor resistance-conferring mutations among clinical isolates of avian H7N9 influenza virus.
Abstract: One strain (A/shanghai/1/2013) contained the R294K substitution in the neuraminidase (NA) gene, indicating resistance to oseltamivir.
Analysis of the full-length genome of a novel strain of the H7N9 avian influenza virus.
PMID: 24940441
2014
Experimental and therapeutic medicine
Result: Resistance gene loci analysis showed that the R294K mutation did not occur in the NA coding protein of the A/Changsha/2/2013 virus and other 50 H7N9 virus strains.
Discussion: Resistance gene loci analysis demonstrated that the R294K mutations of the NA coding protein only occurred in one H7N9 virus strain isolated in Taiwan (A/Taiwan/S02076/2013), suggesting that A/Changsha/2/2013 and 50 other new H7N9 viruses isolated in 2013 were sensitive to neuraminidase inhibitors (e.g.
Resistance to neuraminidase inhibitors conferred by an R292K mutation in a human influenza virus H7N9 isolate can be masked by a mixed R/K viral population.
Introduction: The A/Shanghai/1/2013 isolate has been reported to possess an R292K NA mutation (N2 numbering; R294K for N9 numbering), which is R289K for the novel H7N9 viruses due to the five-amino-acid deletion in the NA stalk region.
IV mutation literature information.
PMID: 
2021
Frontiers in cellular and infection microbiology
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