Plasticity of Amino Acid Residue 145 Near the Receptor Binding Site of H3 Swine Influenza A Viruses and Its Impact on Receptor Binding and Antibody Recognition.
Abstract: Structural analyses revealed that the selected HA mutations (S123G, N460S, and N203V) are away from the F10 epitope but may indirectly impact influenza virus receptor binding, endosomal fusion, or budding.
Abstract: The NA mutation E329K, which was previously identified to be associated with antibody escape, affects the active site of NA, highlighting the importance of the balance between HA and NA function for viral survival.
Glycosylation and an amino acid insertion in the head of hemagglutinin independently affect the antigenic properties of H5N1 avian influenza viruses.
Abstract: The E131N mutation and insertion of leucine at position 134 in the HA protein of the antigenically drifted strains eliminated the reactivity of the virus with the MAbs.
HDAC6 Restricts Influenza A Virus by Deacetylation of the RNA Polymerase PA Subunit.
Method: The following primers were used: PA-K281R-F (5'-GTT CTC AGC GGT CCA GAT TCC TGC TGA TGG AT-3') and PA-K281R-R (5'-ATC CAT CAG CAG GAA TCT GGA CCG CTG AGA AC-3'), PA-K497R-F (5'-AGG AGG GAA GGC GAA GGA CCA ATT TGT ACG G-3') and PA-K497R-R (5'-CCG TAC AAA TTG GTC CTT CGC CTT CCC TCC T-3'), PA-K643R-F (5'-AAC TTT ATT GGC AAG GTC GGT ATT CAA CAG C-3') and PA-K643R-R (5'-GCT GTT GAA TAC CGA CCT TGC CAA TAA AGT T-3'), PA-K664R-F (5'-TCA GCT GAA TCA AGA AGA CTG CTT CTT ATC GTT C-3') and PMID: 30548432
2019
Influenza and other respiratory viruses
Abstract: Even in Japan, no spread of NAI-resistant viruses has been observed, and A/H1N1pdm09 viruses carrying H275Y remain limited.
Abstract: Four of the five mutations in the catalytic sites of A/H1N1pdm09 consisted of H275Y, which was related to high resistance to oseltamivir and peramivir.
Abstract: Most (10/13) of the catalytic site mutations in A/H3N2 were associated with MDCK-passaged induction (D151G/N).
Introduction: These NAIs exert their antiviral function by binding to the enzymatic catalytic sites of influenza surface protein NA.1 In the 2007-2008, oseltamivir-resistant seasonal A/H1N1 viruses carrying NA amino acid (AA) mutation H275Y rapidly spread throughout the world.2
A novel recombinant attenuated Newcastle disease virus expressing H9 subtype hemagglutinin protected chickens from challenge by genotype VII virulent Newcastle disease virus and H9N2 avian influenza virus.
Abstract: Furthermore, a prime-boost vaccination of chickens with rmNA-H9F induced higher levels of NDV- and H9- HI and secretory IgA, as well as reduced viral shedding and virus-induced gross lesions, compared with the commercial vaccine.
Abstract: Remarkably, non-shedding of influenza virus and higher levels of H9 subtype HI titers were observed 7 days post challenge (dpc) in rmNA-H9F vaccinated chickens, than other recombinants.
Abstract: Therefore, in the present work, a cloned full-length copy of the genome of the lentogenic NDV strain rmNA-1 was selected as a backbone vector to construct three chimeric NDVs that expressed (i) the ORF encoding the Abstract: rmNA-H9, rmNA-H9F, and rmNA-H9 (ECTO) stably expressed the modified HA gene for 10 egg passages and the three recombinants were found innocuous to chickens.
In Vitro and In Vivo Characterization of Novel Neuraminidase Substitutions in Influenza A(H1N1)pdm09 Virus Identified Using Laninamivir-Mediated In Vitro Selection.
Abstract: After the generation of single mutants possessing each identified mutation, two A(H1N1)pdm09 recombinants possessing novel NA gene substitutions (i.e., D199E and P458T) were shown to exhibit resistance to more than one NAI.
Abstract: Of note, mutants possessing P458T-which is located outside of the catalytic or framework residue of the NA active site-exhibited highly reduced inhibition by all four approved NAIs.
Abstract: Reverse mutations to the WT were observed in lung homogenate samples from D199E-infected mice after 3 serial passages.
Abstract: We found several novel substitutions in NA (D199E and PMID: 30621708
2019
Virology journal
Conclusion: Moreover, PB2 E627K and PA T97I may play important roles in H7N9 mammal adaption, but the exact role and other substitutions need further verification.
Result: Moreover, E627K substitution in PB2 protein was the common substitution of the three mouse-adapted H7N9 viruses and PA T97I substitution was shared by H7N9-53 MA H7N9-ZSM MA.
Discussion: All these findings demonstrated that though E627K substitution is the common mutation of the three mouse-adapted viruses and it has been proved to increase virulence in mice, it is not the only virulence-determination mutation, there must be other substitutions correlate with PMID: 30640922
2019
PloS one
Abstract: Majority of the samples had some mutations in the NA gene notably: I117M, N248D, and N369K while the amantadine-resistant M mutant, S31N, was found to be absent only in the two sequences collected in 2014.
Method: Samples were considered positive for influenza A and A(H1N)2009 at a threshold cycle below 37 and only those with lower threshold cycles (below 30) were eligible for sequencing.
Discussion:
Discussion: However, some substitutions in the NA gene (I117M, N248D, and N369K) as recorded with the FluSurver (http://flusurver.bii.a-star.edu.sg) might be involved in drug susceptibility.
Detection of influenza A(H3N2) viruses exhibiting reduced susceptibility to the novel cap-dependent endonuclease inhibitor baloxavir in Japan, December 2018.
Discussion: During the Phase II trial, the PA I38T and I38F substitutions emerged after baloxavir treatment in four (3.6%) of 112 A(H1N1)pdm09 viruses isolated from adults aged 20-64 years.
Discussion: Furthermore, influenza A/Victoria/3/75(H3N2) viruses with the PA I38T or I38M substitutions showed 56.6- and 13.8-fold higher EC50 values, respectively.
Discussion: Furthermore, our sequencing analysis revealed that these two PA I38T mutant viruses possessed different PA sequences and thus originated from different viruses, suggesting no human-to-human transmission.
IV mutation literature information.
PMID: 
2019
Journal of virology
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