Virusliterature

IV mutation literature information.

[Epidemiological and genetic characteristics of H5 subtype avian influenza virus in Guangzhou, 2014-2019].

PMID: 32741181 2020 Zhonghua liu xing bing xue za zhi

Abstract: However, mutations of S123P, S133A and T156A occurred, which implied that these strains could tend to bind to human receptors.

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

PMID: 32746754 2020 Emerging microbes & infections

Introduction: A D701N mutation in the PB2 protein led to effective viral replication and enhanced the pathogenicity of both AIVs and swine influenza virus in mammals.

Introduction: A substitution from E to K at position 627 in the PB2 protein significantly increased the pathogenicity of avian influenza viruses (AIVs) in mice.

Result: As shown in Figure 7(A), position of 342 is located near the enzyme active sites at positions 274 and 294 in the NA structure, indicating that an N342D substitution might affect the neuraminidase activity.

Result: Our data show that the neuraminidase enzyme activity of rAH127/NAN34

Functional neuraminidase inhibitor resistance motifs in avian influenza A(H5Nx) viruses.

PMID: 32750468 2020 Antiviral research

Discussion: In the H5N2 background the R292K mutation reduced sensitivity to all three drugs tested as determined by MUNANA assay.

Discussion: In this study we investigated whether known resistance mutations that occur in human isolated IAV strains (E119V, H274Y, R292K and N294S) function to reduce the susceptibility to NAI drugs in the highly pathogenic H5Nx viruses (H5N2, H5N6 and H5N8) that have been responsible for large scale poultry outbreaks in recent years.

Discussion: Investigation of the two viruses carrying these mutations, Y98F (R292K NA mutant) and A189T (N294S

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

PMID: 32786258 2020 ACS chemical biology

Abstract: In the active M2 S31N blockers 1 and 6, the phenyl and isoxazolyl head groups achieve a deeper binding position and high kon/low koff and high kon/high koff rate constants, compared to inactive 2-5, which have much lower kon and higher koff.

Abstract: Infection of cell cultures by influenza virus containing M2 WT or M2 S31N is inhibited by 1-5 or 1-4 and 6, respectively.

Abstract: Study of 1-6 shows that, according to molecular dynamics (MD) simulations and molecular mechanics Poisson-Boltzmann surface area (MM/PBSA) calculations, all bind in the M2 S31N channel with the adamantyl group positioned between V27 and G34 and the aryl group projecting out of the channel with the phenyl (or isoxazole in 6) embedded in the V

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

PMID: 32796071 2020 Journal of virology

Abstract: Analysis of amino acid mutations in the HAs between H7/AH13 and H7/GD16 revealed that L226Q substitution increases the HA binding avidity to sialic acid receptors on red blood cells, leading to decreased HI titers against viruses containing HA Q226 and thus resulting in a biased antigenic evaluation based on HI assay.

Abstract: In this study, we found that the L226Q substitution in HA of A/Guangdong/17SF003/2016 (H7/GD16) increased the viral receptor-binding avidity to red blood cells with no impact on the antigenicity of H7N9 virus.

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

PMID: 32832869 2020 ACS pharmacology & translational science

Abstract: Overall, this is the first systematic study of the drug resistance mechanism of M2-S31N channel blockers using multiple viruses in different cell lines.

Abstract: Recent efforts in drug development against influenza A virus (IAV) M2 proton channel S31N mutant resulted in conjugates of amantadine linked with aryl head heterocycles.

Abstract: The MD simulations show that the V27A, V27F, G34E, and R45H mutations increase the diameter and hydration state of the pore in complex with compound 3.

Abstract: The Molecular Mechanics Generalized Born (MM-GBSA) calculations result in more positive binding free energies for the complexes of resistant M2 (

PMID: 32847862 2020 Journal of virology

Abstract: The E212A mutation may provide structural stability for the epitope, while the substitution G172E probably compensates for loss of fitness introduced by S207R.

Abstract: The results of our experiments supported a critical role for substitution of arginine at position 207 (S207R) in mediating resistance to 53C10, while substitutions at either G172E or E212A did not alter antibody recognition and neutralization.

Profile and generation of reduced neuraminidase inhibitor susceptibility in highly pathogenic avian influenza H7N9 virus from human cases in Mainland of China, 2016-2019.

PMID: 32853849 2020 Virology

Abstract: In presence of NAIs, R238I, A146E, G151E and G234T substitutions were found in HA1 region of HA.

Abstract: Passage with zanamivir induced an E119G substitution in NA, whereas passage with oseltamivir induced R292K and E119V substitutions that simulated that seen in oseltamivir -treated HPAI H7N9 cases, indicating that the high frequency of resistant strains in the HPAI H7N9 isolates is related to NAIs use.

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

PMID: 32873642 2020 Proc Natl Acad Sci U S A

3Introduction: Evolution modes for key mammal-adaptive mutations, including PB2-E627K, were found to differ between LPM- and patient-derived samples, indicating the dynamics of the ""genetic tuning"" of the H7N9 virus in adapting to the mammalian host."

Abstract: Notably, our findings also demonstrate the correlation between rapid host adaptation of H7N9 PB2-E627K and the fatal outcome and disease severity in humans.

Introduction: However, studies on the longitudinal dynamics of the PB2-E627K substitution of the avian-origin virus in infected patients and its influence on disease severity are lacking.

Introduction: However, the adaptive dynamics of PB2-E627K in H7N9 infected patients and the

RNA-seq accuracy and reproducibility for the mapping and quantification of influenza defective viral genomes.

PMID: 32929001 2020 RNA (New York, N.Y.)

Abstract: We further examine the features of DVGs produced by wild-type and transcription-defective (PA-K635A or PA-R638A) influenza viruses, and show an increased diversity and frequency of DVGs produced by the PA mutants compared to the wild-type virus.

Method: Recombinant A/WSN/33 influenza viruses (NCBI:txid382835), either wild-type or bearing single mutations in the PA polymerase subunit (PA-K635A and PA-R638A), were used.

Method: The Illumina library construction and sequencing were performed by the P2M platform at Institut Pasteur.

Result: As shown in Figure 4A,B, DVGs were overall mo

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