Virusliterature

IV mutation literature information.

Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.

PMID: 31305236 2019 The Journal of general virology

Abstract: Here, we identify I292V as the prevalent mutation in PB2 of circulating avian H9N2 and pandemic H1N1 viruses.

Introduction: Here, we identified I292V mutation in PB2 as a dominant genotype in avian H9N2 (since 2010), and in emergent H7N9 and H10N8 viruses; human isolates of such viruses frequently contain the I292V PB2 genotype.

Introduction: The PB2-I292V in H9N2 virus confers increased replication and more severe pathogenicity to mice through enhancing viral polymerase and strong attenuation of IFN-beta induction.

Introduction: Therefore, PB2-I292V is a newly identified mammalian adaptive determinant of

Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.

PMID: 31323237 2019 Antiviral research

Abstract: As part of a 2015-2018 clinical trial of peramivir treatment for acute influenza infections in the elderly, an influenza B/Yamagata/16/1988-like isolate harbouring a Val430Ile neuraminidase (NA) substitution was recovered from a single patient.

Abstract: In NA inhibition assays, oseltamivir, zanamivir and peramivir IC50s of the Val430Ile isolate were 4-, 15- and 16-fold higher compared to a wild-type (WT) strain.

Abstract: In reverse genetics experiments, the Ile430Val reversion restored the drug susceptible phenotype.

Abstract: Molecular dynamics simulations suggested that Val430Ile impacts the NA binding through a mechanism involvin

Biological properties of influenza A virus mutants with amino acid substitutions in the HA2 glycoprotein of the HA1/HA2 interaction region.

PMID: 31329089 2019 The Journal of general virology

Abstract: However, the HA2 mutation V662H and double mutation T642H, V662H shifted the fusion pH maximum to lower values (ranging from 5.1 to 5.3) compared to pH from 5.4 to 5.6 for the wild-type and 64 mutant.

Abstract: We prepared mutants of neurotropic IAV A/WSN/33 (H1N1) with aa substitutions in HA2 gp at the site of HA1/HA2 interaction, namely T642H (HA2 numbering position 64, H1 numbering position HA407; referred to as mutant '64'), V662H ('66') (HA409); and a double mutant ('D') with two aa substitutions (T642H,

Rapid isolation of a potent human antibody against H7N9 influenza virus from an infected patient.

PMID: 31336147 2019 Antiviral research

Abstract: Additionally, the 3L11 escape strains had G151R (Gly151 Arg151) and S152P (Ser152 Pro152) mutations within a conserved antigenic site A near the RBS that were not observed in field strains.

Evolution of H9N2 low pathogenic avian influenza virus during passages in chickens.

PMID: 31351233 2019 Infection, genetics and evolution

Abstract: For example, the amino-acid substitution N337K in the haemagglutinin (HA) cleavage site region detected in the 6th passage as low frequency variant had undergone rapid selection and became predominant in the 7th passage.

Severe cases of seasonal influenza in Russia in 2017-2018.

PMID: 31356626 2019 PloS one

Abstract: One strain of influenza virus A(H1N1)pdm09 was resistant to oseltamivir and had the H275Y amino acid substitution in the NA protein.

Abstract: This study demonstrated the importance of monitoring D222G/N polymorphism, including detection of minor viral variants with the mutations, in the hemagglutinin gene of A(H1N1)pdm09 for epidemiological surveillance.

Discussion: Among the 87 analyzed isolates of influenza A and B viruses, only one A(H1N1)pdm09 strain isolated from a lethal case of influenza was resistant to oseltamivir while remaining susceptible to zanamivir; it contained the H275Y amino acid substitution in the NA protein.

Discussion: Analysis of the presence of minor variants of the mutations revealed simultaneous presence of the virus varian

Naturally occurring mutations in PB1 affect influenza A virus replication fidelity, virulence, and adaptability.

PMID: 31366399 2019 Journal of biomedical science

Abstract: These results suggest that the PB1-S216G substitution enhances viral epidemiological fitness by increasing the frequency of adaptive mutations in human influenza A/H1N1 viruses.

Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.

PMID: 31382442 2019 Viruses

Abstract: Although N166D did not significantly affect viral replication in Madin-Darby canine kidney (MDCK) cells and viral shedding in the larynx and cloaca of chicken, N166D attenuated the pathogenesis of the virus in mice.

Abstract: Considering the field strains of H9N2 with N166D mutation are frequently isolated in the countries with H9N2 vaccination, the findings that the single mutation in HA, N166D, affected both the antigenicity and pathogenesis of H9N2 highlight the significance of surveillance on such mutation that may contribute to the failure of H9N2 vaccination in the field.

Abstract: In this study, seven critical sites in HA associated with the antigenicity were identified and the effects of a HA mutation (

The evolution and characterization of influenza A(H7N9) virus under the selective pressure of peramivir.

PMID: 31400550 2019 Virology

Abstract: The NA-H274Y variant showed decreased replicative fitness at the early stage of infection accompanied with impaired NA function.

Abstract: Two important amino acid substitutions were identified in NA, I222T and H274Y, which caused reduced susceptibilities to oseltamivir or both oseltamivir and peramivir as confirmed by enzyme- and cell-based assays.

The neuraminidase of A(H3N2) influenza viruses circulating since 2016 is antigenically distinct from the A/Hong Kong/4801/2014 vaccine strain.

PMID: 31406333 2019 Nature microbiology

Abstract: This antigenic drift was mainly caused by amino acid mutations at NA residues 245, 247 (S245N/S247T; introducing an N-linked glycosylation site at residue 245) and 468.

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