Result: For the NA protein, a T16A substitution occurs at a site located in the transmembrane region of this protein (Figure 4).
Result: Given the role of the NS1 protein in suppressing host cellular immune responses, the NS1-E227K mutation might be a molecular determinant to hone the function of the immune suppression by H3N2 CIV.
Result: However, it is interesting to note that 11 out of the 54 (20.37%) effective substitutions in H3N2 CIV, including HA-G146S, HA-V242I, HA-V418I, M1-V15I, M2-
Novel Clade 2.3.4.4b Highly Pathogenic Avian Influenza A H5N8 and H5N5 Viruses in Denmark, 2020.
Abstract: Genetic analyses of one of the H5N8 viruses revealed the presence of a substitution (PB2-M64T) that is highly conserved in human seasonal influenza A viruses.
Result: In addition, one of the H5N8 viruses (A/barnacle goose/Denmark/14139-3/2020) had a PB2-M64T amino acid substitution that is highly conserved in human influenza A H1N1, H2N2, and H3N2 viruses.
Result: The PB2-M64T substitution was not present in A/Astrakhan/3212/2020(H5N8) (EPI_ISL_1038924) virus detected in workers at a poultry farm in Russia on 12 December 2020.
Discussion: The genetic characterization revealed that one of the Danish H5N8 viruses contained a PB2-M64T substitution.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: The 2018 virus harbored amino acid mutations (I123V and N205S) in important functional sites; however, 108R and 189G were highly conserved between A/California/07/2009 and the 2018 variant.
Abstract: To better understand interactions between influenza viruses and the human innate immune system, we generated and rescued seasonal 2009 H1N1 IAV mutants expressing an NS1 protein harboring a dual mutation (R108K/G189D) at these conserved residues and then analyzed its biological characteristics.
Introduction: Here, we sequenced a seasonal 2009 H1N1 influenza virus isolated in 2018 and confirmed the presence of mutations I123V and N205S in important functional sites.
Introduction: However, the NS
Molecular Characterization of Seasonal Influenza A and B from Hospitalized Patients in Thailand in 2018-2019.
Result: Additional amino acid substitutions were found at P99S, C123S, and S139C for segment NA, T285I for segment M, and V453A at the NP segment (Tables S7 and S8).
Result: Among these Thai strains, we found additional mutations at antigenic sites; S91R (Cb), S181T(Sa), and T202I (Sb) (Figure 2B).
Result: Determination of amino acid substitutions among the A/H1N1 isolates also revealed the mutation Q51K, F74S, G77R, V81A, I188T
Identification of H3N2 NA and PB1-F2 genetic variants and their association with disease symptoms during the 2014-15 influenza season.
Abstract: In human nasal epithelial cell cultures, a virus with the novel NAg+F2P genotype replicated less well compared with a virus with the parental genotype.
Abstract: Retrospective analyses of clinical data showed that NAg+F2P genotype viruses were associated with increased cough and shortness of breath in infected patients.
Abstract: The NA and PB1-F2 mutations were present in a subset of clade 3C.2a viruses (NAg+F2P), which dominated during the subsequent influenza seasons.
Abstract: The isolates were classified by HA clade and the presence of a new set of co-selected mutations in NA (a glycosylation site, NAg+) and PB1-F2 (H75P).
Method: A/Colu
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Result: Figure 2 represents snapshot images obtained from the MD simulations for the WT and H274Y mutant NA-OTV complexes, showing the OTV binding site and the region adjacent to residue 274.
Result: Figure 3 shows the dRIN graphs for the WT and H274Y mutant NA complexed with OTV.
Result: Figure 4B indicates that the occupancy of ligand-residue interactions between the OTV and its surrounding residues, E119, D151, R152, and S246 decreased after H274Y mutation, whereas the occupancy of the OTV-Y406 interaction increased.
Result: Figure 4B shows the change in the occupancies of residues interacting with each of the WT and H274Y mutant
Result: dRIN of H274Y mutant NA.
Genetic characterisation of the influenza viruses circulating in Bulgaria during the 2019-2020 winter season.
Abstract: The HA genes of A(H3N2) viruses analysed belonged to clades 3C.3a (21 strains) and 3C.2a (5 strains): subclades 3C.2a1b + T131K, 3C.2a1b + T135K-B and 3C.2a1b + T135K-A.
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
Abstract: More importantly, after 5 passages in mice, the virus acquired two adaptive mutations, PB1-H115Q and B2-E627K, exhibiting increased virulence and aerosol transmissibility.
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.
Discussion: The G622D mutation of the PB1 p
In Vivo Therapy with M2e-Specific IgG Selects for an Influenza A Virus Mutant with Delayed Matrix Protein 2 Expression.
Abstract: Deep sequencing analysis of viral RNA isolated at different time points after treatment revealed that the sequence variation in M2e was limited to P10H/L and/or I11T in anti-M2e MAb-treated mice.
Introduction: Although only the M2e sequence was thoroughly investigated in this study, 6 synonymous and 2 nonsynonymous mutations (A127T and V228L) were also detected in M1.
Introduction: In one instance, resistance was acquired by a glutamic acid to glycine residue mutation at position 8 in M2e (and M1), which resulted in loss of anti-M2e IgG binding.
Method: Determination of M2e sequence in viral stocks of PR8, PR8-M2-P10H, PR8- PMID: 34242774
2021
Infection, genetics and evolution
Abstract: Molecular simulations found that the mutations (V135T, S145P, and L226Q) around the HA receptor pocket increased the affinity to alpha2,3-linked sialic acid (SIA) while decreased to alpha2,6-linked SIA.
IV mutation literature information.
PMID: 
2021
Frontiers in microbiology
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