Abstract: We observed escape mutations on the head domain of the N1 protein around the enzymatic site (S364N, N369T, and R430Q) and also detected escape mutations located on the sides and bottom of the NA (N88D, N270D, and Q313K/R).
N-Glycolylneuraminic Acid Binding of Avian and Equine H7 Influenza A Viruses.
Abstract: The additional mutations S128T, I130V, T189A, and K193R converted the specificity from NeuAc to NeuGc.
Abstract: We found that the A135E mutation is key for binding alpha2,3-linked NeuGc but does not abolish NeuAc binding.
Discussion: Here, we demonstrate that avian H7 and H15 HAs can bind both NeuAc and NeuGc by the introduction of A135E.
Discussion: Nevertheless, here we demonstrated that avian H7 and H15 HAs, although genetically distinct from equine H7 viruses, are able to bind NeuGc after the introduction of mutation A135E.
Discussion: We previously studied the NeuAc-specific HA of A/Vietnam/1203/2004 H5N1 (H5VN) and its Y161A mutant th
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: Here, we identified a new helper mutation, Y276F, that can rescue the functional defects of H275Y and contribute to the evolution of drug resistance in IAV.
Abstract: In prior work, we identified a hyperactive mutation (Y276F) that increased NA activity by approximately 70%.
Abstract: In this study, we measured the relative fitness, NA activity, and surface expression, as well as sensitivity to oseltamivir, for several oseltamivir resistance mutations, including H275Y in the wild-type and Y276F genetic background.
Abstract: Our results demonstrate that Y276F selectively rescues the fitness defect of H275Y by restoring its
The Species-Specific 282 Residue in the PB2 Subunit of the Polymerase Regulates RNA Synthesis and Replication of Influenza A Viruses Infecting Bat and Nonbat Hosts.
Abstract: Introduction of E282S mutation in the human-adapted PB2 (influenza A/H1N1/WSN/1933) drastically reduces polymerase activity and replication efficiency of the virus in human, bat, and canine cells.
Genetic and biological properties of H10N3 avian influenza viruses: A potential pandemic candidate?
PMID: 35067005
2022
Transboundary and emerging diseases
Abstract: Importantly, several key molecular markers associated with mammalian adaptation had been detected in both avian and human-isolated H10N3 influenza viruses in the HA (G228S), PB2 (I292V and A588V), PB1 (M317V and I368V), and PA (A343S, K356R and S409N) protein.
Acetylation of the influenza A virus polymerase subunit PA in the N-terminal domain positively regulates its endonuclease activity.
Abstract: Notably, the substitution of the lysine residue at position 19 with glutamine, a mimic of the acetyl-lysine residue, enhanced its endonuclease activity in vitro; this point mutation also accelerated influenza A virus RNA-dependent RNA polymerase activity in the cell.
Interactions between Influenza A Virus Nucleoprotein and Gene Segment Untranslated Regions Facilitate Selective Modulation of Viral Gene Expression.
Abstract: We previously demonstrated that a single substitution in the viral nucleoprotein (NP:F346S) selectively modulates neuraminidase (NA) gene segment expression while leaving other segments largely unaffected.
Abstract: While the NP:F346S substitution did not significantly alter the RNA binding or oligomerization activities of NP in vitro, it specifically decreased the ability of NP to promote NA segment viral RNA (vRNA) synthesis.
Identification of a Permissive Secondary Mutation That Restores the Enzymatic Activity of Oseltamivir Resistance Mutation H275Y.
Abstract: Mutations were found in HA (A135 T, T136S, and T160 A [H3 numbering]), M1 (N30D and T215 A), NS1 (P42S and D97 E), PB2 (R389 K), and PA (N383D) proteins; these mutations have been shown to be related to mammalian adaptation and changes in virulence of AIVs.
Discussion: In this study, no key amino acid mutations were found in PB2, especially the E627 K and D701 N mutations, which have b
IV mutation literature information.
PMID: 
2022
Journal of virology
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