Abstract: Four residues in the N-terminal region of PA are critical in mediating the PB2 E627K acquisition.
Abstract: Furthermore, the impaired viral polymerase activity of H7N9 AIV caused by the depletion of ANP32A led to reduced virus replication in Anp32a-/- mice, abolishing the acquisition of the PB2 E627K mutation and instead driving the virus to acquire the alternative PB2 D701N mutation.
Abstract: H7N9 AIVs that emerged in 2013 possess a prominent ability in gaining the PB2 E627K mutation in humans.
Abstract: Here, we demonstrate that the acquisition of the H7N9 PB2
Genetic and Phylogenetic Characterization of the M Gene of Influenza A Virus Isolated from Iranian Patients.
PMID: 31223581
2019
Iranian journal of public health
Abstract: Amino acid seq
Result: All Iranian H1N1 and H3N2 studied isolates possessed the most frequently adamantane-drug resistance mutation resulted in the amino acid substitution S31N in the M2 protein.
Discussion: However, some limited studies carried on Iranian isolates got from 2005 to 2008 have demonstrated the prevalence of amantadine-resistance A (H3N2) mutants, all resulted in the amino acid substitution S31N in the M2 protein.
Discussion: The present study showed that all strains of H1N1 and H3N2 subtypes contained the amino acid substitutions S31N, as expected.
Discussion: The single point mutation at position 31 (S31N) is common and has been identified as the most frequent adamantine-resistant A (H3N2 and H1N1) viruses distributed across the world.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: In contrast, V116A, I117V, E119A, and N295S substitutions resulted in significantly lower viral titers (1.2 logs) than the parental CA/04 virus in NHBE cells.
Abstract: The efficiencies of NAs with E119A, H275Y, and N295S mutations to catalyze all substrates were ~19.4% of the CA/04 NA.
Abstract: Two NA mutations, V116A and I117V, are found in ~0.6% of human, avian, and swine N1 isolates.
Abstract: Using the A/California/04/09-like (CA/04, H1N1) background, we examined the impact of V116A and
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: A third group retained the I106M, but had a compensating R363K substitution, which regained almost wild type NA properties.
Abstract: The I106M may impact NA function through steric effects on the movement of the 150 and 430-loops.
Abstract: The I106M substitution was unstable, with progeny rapidly reverting to wild type by three different mechanisms.
Abstract: The I106M viruses had similar replication kinetics in MDCK cells as wild type viruses, but their ability to bind to and infect CHO-K1 cells expressing high levels of cell-bound mucin was compromised.
Abstract: These had a novel non-active site I106M substitution in the NA gene, but un
Highly pathogenic avian influenza H7N9 viruses with reduced susceptibility to neuraminidase inhibitors showed comparable replication capacity to their sensitive counterparts.
Abstract: CONCLUSIONS: All 4 amino acid substitutions (R292 K, E119V, A246T or H274Y) in NA reduced the susceptibility of HPAI H7N9 to NAIs.
Abstract: RESULTS: Four potential NAI resistance sites, R292 K, E119V, A246T or H274Y, were screened.
Method: A virus containing amino acid substitutions in sites related to potentially reduced susceptibility to NAIs in HPAI H7N9 viruses, including R292 K, E119V,
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Discussion: A previous study found that the substitution of N319K in NP protein was located on the surface at the right-hand side of the nucleoprotein body domain and resulted in an increase of polymerase activity.
Discussion: Dual mutations K305R + V313F increased the fatality of the viruses.
Discussion: Furthermore, when compared to that of rgHuN-WT, the occurrence of a single substitution V313F or K305R increased viral pathogenicity in mice, while K357Q obviously reduced the viral pathogenicity.
Discussion: However, the introduction of the K305R into dual mutation K305R + V313F led to a
A Single Amino Acid Substitution at Residue 218 of Hemagglutinin Improves the Growth of Influenza A(H7N9) Candidate Vaccine Viruses.
Abstract: By introducing a single adaptive substitution, G218E, into the hemagglutinin (HA), we generated reassortant A(H7N9)-G218E CVVs that were characterized by significantly enhanced growth in both cells and eggs.
Abstract: In contrast, the G218E-mediated growth improvement was attributed to relatively balanced HA and NA functions, resulted from reduced HA binding to both human- and avian-type receptors, and thus facilitated NA-mediated virus release.
Abstract: The in vitro and in vivo experiments demonstrated comparable antigenicity of the G218E CVVs with that of their wild-type (WT) counterparts, and both the WT and the
Serial Section Array Scanning Electron Microscopy Analysis of Cells from Lung Autopsy Specimens following Fatal A/H1N1 2009 Pandemic Influenza Virus Infection.
Abstract: A/H1N1/pdm09 harboring the D222G substitution has a receptor-binding preference for alpha-2,3-linked sialic acids expressed on human AECs and infects them in the same way as H5N1 and H7N9 avian IAVs.
Abstract: This was because the majority of A/H1N1/pdm09 in the lung tissue harbored an aspartic acid-to-glycine substitution at position 222 (D222G) of the hemagglutinin protein.
Introduction: Since the first appearance of A/H1N1/pdm09, an amino acid substitution from aspartic acid to glycine at position 222 (D222G) in the HA protein has been identified sporadically
Discussion: A/H1N1/pdm09-D222G proliferated in the lung, and many viral antigens and much viral RNA were detected in AEC-IIs.
A cross-reactive human monoclonal antibody targets the conserved H7 antigenic site A from fifth wave H7N9-infected humans.
Abstract: By generating escape mutant variants, we found that a single G151E substitution in the viral H7 antigenic site A could abort the neutralizing activity.
IV mutation literature information.
PMID: 
2019
Infection, genetics and evolution
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