IV mutation literature information.


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 33914831       2021       PloS one
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


  Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
 PMID: 33933515       2021       Antiviral research
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.
 PMID: 34020222       2021       Biosensors & bioelectronics
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).
 PMID: 33713731       2021       Antiviral research
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.


  Changes in sialic acid binding associated with egg adaptation decrease live attenuated influenza virus replication in human nasal epithelial cell cultures.
 PMID: 33985852       2021       Vaccine
Abstract: In the 2012-2013 northern hemisphere vaccine, the H3N2 HA vaccine strain contained three amino acid changes - H156Q, G186V and S219Y - which altered HA antigenic structure and thus presumably decreased vaccine efficacy.


  Interplay between H1N1 influenza a virus infection, extracellular and intracellular respiratory tract pH, and host responses in a mouse model.
 PMID: 33979408       2021       PloS one
Method: The local immune responses of mice infected with WT or Y17H IAVs were measured and compared with those of PBS-treated mice.
Method: We divided the mice into three groups of five and intranasally inoculated them with 30 muL of the acid-stable 2009 pandemic H1N1 virus (WT 750), acid-destabilized H1N1 virus (HA1-Y17H 750 or HA1-Y17H 375K), or PBS.
Method: We inoculated mice with 750 PFU HA1-Y17H, 750 PFU WT, or 375,000 PFU HA1-H17H.
Method: Wild-type A/Tennessee/1-560/2009 (H1N1), A/California/04/09 (H1N1), and A/England/195/2009 (H1N1) have been reported to have HA activation pH values of 5.5, while the



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