Genetic sequencing of influenza A (H1N1) pdm09 isolates from South India, collected between 2011 and 2015 to detect mutations affecting virulence and resistance to oseltamivir.
PMID: 33154243
2020
Indian journal of medical microbiology
Abstract: All the study isolates possessed H274 residue and 7 strains had N295S, the next most common mutation found in oseltamivir-resistant variants.
Abstract: Conclusion: In this study, although H274Y mutation associated with oseltamivir resistance has not been noted, significant mutations have been noted in both HA and NA genes including D239N, N295S, V106I, Q136K, N248D, V267A.
Abstract: Two samples collected from expired patients had D239N (D222G or D225G) mutation in HA.
Adsorptive mutation and N-linked glycosylation modulate influenza virus antigenicity and fitness.
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.
Result: Finally, in the high avidity SKP-827/16 T180 V background virus, the addition of N-linked glycans was similar to their effect in SKP-827/16 T180 virus, such that N148 facilitated significantly greater viral titers in MDCK and CK cells (Figure 3(C,F)).
Result: Finally, in the highest avidity SKP-827/16 T180 V background, N148 was again shown to completely ablate binding to 6SLN and 3SLN while reducing binding towards 3SLN(6Su) (Figure 2(K)).
Result: However, in CK cells addition of N-linked glycans at residues 134 and 189 let to comparable virus replication kinetics with non-glycosylated SKP-827/16 T180 V
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.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
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.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
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
IV mutation literature information.
PMID: 
2020
Indian journal of medical microbiology
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