Abstract: We utilize the H9N2 A/chicken/Pakistan/SKP-827/16 virus which naturally contains HA residue T180 that we have previously shown to be an adsorptive mutant relative to virus with T180A.
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.
Discussion: In fact, the addition of N148 to virus with any avidity background led to reduced binding avidity to all tested receptor analogues and a significant impact on virus replication apart from T180A viruses in MDCK cells.
Discussion: In the data presented here, it is plausible that an H9N2 virus could escape immunity through addition of an N-linked glycan at residues 134, 148 or 189 and
Identification of Novel Influenza Polymerase PB2 Inhibitors Using a Cascade Docking Virtual Screening Approach.
Abstract: Among these, four compounds (11D4, 12C5, 21A5, and 21B
Conclusion: Among these, four compounds, namely, compound 11D4, 12C5, 21A5, and 21B1, could inhibit a broad spectrum of influenza virus strains, including HK/68 (H3N2), A/WSN/33 (H1N1), ZX/1109 (H1N1, natural isolate, oseltamivir-resistant), the PR/8-R292K mutant (H1N1, recombinant oseltamivir-resistant strain), and the influenza B/Lee/40 virus.
Result: Except for compound 21B1 showing no activity against the A/Hong Kong/8/68 (HK/68, H3N2) strain, these compounds were active against a variety of influenza A virus strains, including HK/68 (H3N2), A/WSN/33 (H1N1), A/LiaoNing-ZhenXing/1109/2010 (ZX/1109, H1N1, natural isolate oseltamivir-resistant), the PR/8-R292K mutant (H1N1, recombinant oseltamivir-resistant), the PR/8-I38T mutant (H1N1, recombinant baloxavir-resistant), and influenza B/Lee/40 virus strains (Table 1).
Host ANP32A mediates the assembly of the influenza virus replicase.
Method: pcDNA-huANP32A 176-183, pcDNA-PB2 T609A, pcDNA-PB2 P132A, pcDNA-PA D529A/R531A/E533A, pcDNA-PA K413A, pcDNA-PA K324A/H326A/E327A and pcDNA-PA K339A/Q340A were generated from pcDNA-huANP32A, pcDNA-PB2 and pcDNA-PA by site-directed PCR mutagenesis and validated by Sanger sequencing.
Mutations in PB1, NP, HA, and NA Contribute to Increased Virus Fitness of H5N2 Highly Pathogenic Avian Influenza Virus Clade 2.3.4.4 in Chickens.
Abstract: The reassortant virus with the HA and NA from the chicken virus, where mutations in functionally known gene regions were acquired as the virus circulated in turkeys (HA S141P and NA S416G) and later in chickens (HA M66I, L322Q), showed faster virus growth, bigger plaque size and enhanced heat persistence in vitro, and increased pathogenicity and transmissibility in chickens.
Abstract: Viruses with the wild bird virus backbone and either PB1, NP, or the entire polymerase complex of the chicken isolate, caused higher and earlier mortality in chickens, with three mutations ( PMID: 33270431
2020
ACS sensors
Abstract: Using the developed method, we successfully identified SARS-CoV-2, pH1N1, and pH1N1/H275Y viruses by the naked eye.
Introduction: For the colorimetric detection of SARS-CoV-2, pH1N1, and pH1N1/H275Y, viral lysates and biotin-protospacer adjacent motif (PAM)-presenting oligonucleotide (PAMmer) were added to dCas9/gRNA-attached well plates, followed by the horseradish perox
Method: SARS-CoV-2 (BetaCoV/Korea/KCDC03/2020) and pH1N1/H275Y mutant virus (H275Y mutation; A/Korea2785/2009 pdm: NCCP 42017) were provided by the National Culture Collection for Pathogens (NCCP), which is operated by the Korea National Institute of Health.
Method: pH1N1 and pH1N1/H275Y virus titers were determined using a one-step real-time PCR kit (Promega, Madison, WI) in accordance with the manufacturer's instructions.
[The Effect of I155T, K156Q, K156E and N186K Mutations in Hemagglutinin on the Virulence and Reproduction of Influenza A/H5N1 Viruses].
Abstract: Amino acid substitutions I155T, K156Q, K156E+V138A, N186K led to a decrease in thermal stability, replication activity of the mutant viruses in chicken embryos, and virulence for mice, although these effects differed between the variants.
Abstract: The A138V and N186K mutations seem to be adaptive in mammalian viruses.
Abstract: The analysis of the frequency of these mutations in natural isolates of H5N1 influenza viruses indicated that the K156E/Q and N186K mutations have little chance to gain a foothold during evolution, in contrast to the I155T mutation, which is the most responsible for antigenic drift.
Altering Intracellular Localization of the RNA Interference Factors by Influenza A Virus Non-structural Protein 1.
Abstract: We found that the single residue substitution of aspartic acid with histidine at position 101 (D101H) of IAV-PR8 NS1 was sufficient to induce the nuclear import process and to enhance the virulence of IAV-PR8 in mice.
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.
Method: The lungs of BALB/c mice inoculated intranasally with PR8 WT, PR8 D101H, or PBS were harvested 3 d.p.i., fixed in 10% neutral-buffered formalin, transferred to 70% alcohol, and embedded in paraffin.
The Effect of I155T, K156Q, K156E and N186K Mutations in Hemagglutinin on the Virulence and Reproduction of Influenza A/H5N1 Viruses.
Abstract: Amino acid substitutions I155T, K156Q, K156E+V138A, N186K led to a decrease in thermal stability, replication activity of the mutant viruses in chicken embryos, and virulence for mice, although these effects differed between the variants.
Abstract: The A138V and N186K mutations seem to be adaptive in mammalian viruses.
Abstract: The analysis of the frequency of these mutations in natural isolates of H5N1 influenza viruses indicated that the K156E/Q and N186K mutations have little chance to gain a foothold during evolution, in contrast to the I155T mutation, which is the most responsible for antigenic drift.
In silico analysis and molecular characterization of Influenza A (H1N1) pdm09 virus circulating and causing major outbreaks in central India, 2009-2019.
PMID: 33604005
2020
Iranian journal of microbiology
Result: Analysis of amino acid sequence alignment revealed changes at two positions (T151A, D239G) at RBS of HA between genogroup 2 and 3, three positions (A151T, S200P, S202T) between genogroup 3 and 4, two positions (N114D, E279G) between 4 and 6A, four positions (N101S, Q180K, G279E, E300K) between 6A and 6B, three positions (S101N, K180Q, I251V) between 6B and 6C genogroup, four positions (G101S, T214A
Mutations in PB2 and HA enhanced pathogenicity of H4N6 avian influenza virus in mice.
PMID: 31081750
2020
The Journal of general virology
Abstract: Although individual L331I or G453R substitutions in HA did not change the pathogenicity of BJ21 in mice, both mutations significantly enhanced virulence.
Abstract: Further studies showed that the introduction of E158K and/or E627K substitutions into PB2 significantly increased polymerase activity, which led to the enhanced replication and virulence of BJ21-MA.
Abstract: Molecular analysis of BJ21-MA identified four mutations, located in proteins PB2 (E158K and E627K) and HA (L331I and G453R, H3 numbering).
IV mutation literature information.
PMID: 
2020
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