Abstract: As expected, PB1-L66V showed at least two-times-lower mutation rates and decreased misincorporation rates, compared to the wild type (WT).
Abstract: Consequently, we identified a Leu66-to-Val single amino acid mutation in polymerase basic protein 1 (PB1).
Abstract: In this study, we isolated a novel influenza virus strain with a Leu66-to-Val single amino acid mutation in PB1 that displayed a significantly higher fidelity than the WT.
Abstract: The PB1-
Abstract: The high-fidelity phenotype of PB1-L66V was confirmed using next-generation sequencing analysis and biochemical assays with the purified influenza viral polymerase.
PB1 S524G mutation of wild bird-origin H3N8 influenza A virus enhances virulence and fitness for transmission in mammals.
Abstract: Co-occurrence of the mutations D222G and D222N was detected in a substantial number of the studied fatal cases (41%).
Abstract: The D222G/N mutations in the hemagglutinin (HA) gene of A(H1N1)pdm09 are associated with severe and fatal human influenza cases.
Abstract: The D222G/N mutations were detected at a low frequency (less than 1%) in the rest of the studied samples from fatal and nonfatal cases of influenza.
Abstract: The high rate of occurrence of HA D222G/N mutations in A(H1N1)pdm09 viruses, their increased ability to replicate in the LRT and their association with fatal outcomes points to the importance of monitor
An influenza A(H5N8) virus isolated during an outbreak at a poultry farm in Russia in 2017 has an N294S substitution in the neuraminidase and shows reduced susceptibility to oseltamivir.
Abstract: An NA-N293/294S substitution was not present in sequences from the GISAID database.
Abstract: Fewer than 1% of analyzed viruses had amino acid substitutions associated with reduced susceptibility to baloxavir (PA-E199G, PA-E199E/G) or reduced or highly reduced inhibition by neuraminidase inhibitors (NA-R150/152K, NA-I221/222M, NA-I221/222I/M, NA-I221/222V, NA- PMID: 33941189
2021
BMC biology
Discussion: The protective activity of MX1 against IAV was originally discovered in A2G mice that carry a wild-type Mx1 allele.
Discussion: The wild type functional Mx1 allele has been transferred from A2G to C57BL/6 mice to generate strain B6.A2G-Mx1r/r (B6-Mx1r/r).
The PB2 co-adaptation of H10N8 avian influenza virus increases the pathogenicity to chickens and mice.
PMID: 34008327
2021
Transboundary and emerging diseases
Abstract: Among them, PB2-A588V significantly enhanced the activity of polymerase in avian and mammalian cells.
Abstract: In this study, we found that the mutations of PB2-I292V, PB2-R389K, PB2-A588V, PB2-T598M/V, PB2-L648V, and PB2-T676M substitutions significantly increased after 2012.
Abstract: Notably, animal experiments showed that PB2-A588V substitution increased the pathogenicity and transmissibility
Double mutations in the H9N2 avian influenza virus PB2 gene act cooperatively to increase viral host adaptation and replication for human infections.
PMID: 34061017
2021
The Journal of general virology
Abstract: K526R, E627V or E627K), indicating a host adaptation advantage for these double mutations.
Abstract: Most of the relevant human virus isolates carry the PB2-A588V mutation together with another PB2 mutation.
Evolution of the PB1 gene of human influenza A (H3N2) viruses circulating between 1968 and 2019.
PMID: 34033262
2021
Transboundary and emerging diseases
Abstract: In contrast, the backward mutant, A113V/R586K/N619D/I709V, reduced polymerase activity in human cells.
Abstract: The PB1 I709V decreased viral replication in vitro, but this mutant only showed less effect on mice infection experiment, which suggested influenza A virus evolved in human host was not always consisted with highly replication efficiency and pathogenicity in other mammalian host.
Abstract: The PB1 V709I or PB1 V113A/K586R/D619N/V709I induced higher polymerase activity of HK/68 in human cel
Development of 6E3 antibody-mediated SERS immunoassay for drug-resistant influenza virus.
Abstract: Furthermore, it was immobilized on Au nanoplate and nanoparticles, enabling surface-enhanced Raman scattering (SERS)-based detection of the H275Y mutant pH1N1.
Abstract: Here we report a novel 6E3 monoclonal antibody capable of recognizing and binding to the H275Y neuraminidase (NA) mutation, which has been associated with reduced susceptibility of influenza viruses to NA inhibitors.
Abstract: Molecular modeling studies also suggest the high-affinity binding of this antibody to pH1N1 H275Y NA.
Abstract: The 6E3 antibody had a KD of 72.74 muM for wild-type NA and 32.76 pM for H275Y NA, suggesting that
Secondary substitutions in the hemagglutinin and neuraminidase genes associated with neuraminidase inhibitor resistance are rare in the Influenza Resistance Information Study (IRIS).
Abstract: All cultured viruses with the known resistance substitutions H275Y or R292K showed reduced susceptibility to oseltamivir in the NA-star assay.
Abstract: Known resistance substitutions were detected by mutation specific RT-PCR in viruses of 57 of 1803 (3.2%) oseltamivir-treated individuals, including 39 individuals infected with A/H1N1pdm09 [H275Y] virus and 18 with A/H3N2 [R292K] virus.
Abstract: Only in two A/H1N1pdm09 [H275Y] viruses, the potentially compensatory secondary substitutions HA-D52N and NA-R152K were detected.
IV mutation literature information.
PMID: 
2021
Journal of virology
Browser Board
Co-occurred Entities
Filtrator
ViMRT