Abstract: Genomic analysis revealed mutations in the PB2 (E192K and D701N), PB1 (F269S, I475V, and L598P), HA (V242E), NA (G170R), and M1 (M192V) proteins.
Identification of Rare PB2-D701N Mutation from a Patient with Severe Influenza: Contribution of the PB2-D701N Mutation to the Pathogenicity of Human Influenza.
Abstract: An exhaustive search has revealed PB2-D701 as a highly conserved position in all available H1N1 human virus sequences in NCBI database, showing a very low prevalence of PB2-D701N change.
Abstract: Several amino acid changes have been previously implicated in adaptation of avian influenza viruses to human hosts, among them the D701N change in the PB2 polymerase subunit that also is the main determinant of avian virus pathogenesis in animal models.
Abstract: This study helps to clarify a debate that has arisen regarding the role of PB2-D701N in human influenza virus pathogenicity.
Introduction: A search in the NCBI Influenza Virus Resource database2 indicated that NA-
Co-expression of sialic acid receptors compatible with avian and human influenza virus binding in emus (Dromaius novaehollandiae).
Abstract: Since 2006, several reports of IAV isolations from emus have surfaced and avian influenza infection of emus can lead to the selection of mammalian like PB2-E627K and PB2-D701N mutants.
PB2-588 V promotes the mammalian adaptation of H10N8, H7N9 and H9N2 avian influenza viruses.
Introduction: Another well-known substitution D701N in PB2 is primarily found in a duck H5N1 virus that was highly pathogenic to mice.
Discussion: Many adaptive mutations in PB2, such as E627K, D701N, K526R, and T271A have been proven to be important for different avian influenza viruses to break the host species barrier to infect mammals.
Discussion: Previous studies have shown that D701N and E627K may influence the interaction of PB2 with different isoforms of importin-alpha to adapt mammalian hosts and a recent study showed that the PB2-627K resists the signaling-independent antiviral effect
Genomic Signatures for Avian H7N9 Viruses Adapting to Humans.
Conclusion: We used a reporter assay to test all of these substitutions and showed that either Q591K, M535L, or D701N mutation increases the viral RNP activity in human cells with PB2 627E, suggesting that E627K, Q591K, M535L, and D701N are crucial markers for assessing the potential of an avian virus to infect humans, as well as for potentially increasing adaptation for the virus to gain human-to-human transmission capability in leading to a pandemic in the future.
Table: D701N
Discussion: In
Discussion: In all, 15 D701N substitutions were observed, and none occurred after January 2014.
Amino acid changes in PB2 and HA affect the growth of a recombinant influenza virus expressing a fluorescent reporter protein.
Result: In fact, the PB2-D701N and PB2-S714R mutations facilitate adaptation of avian influenza viruses to mammals by affecting the PB2 interaction with importin, resulting in better exposure of the PB2 nuclear localization signal.
Novel Polymerase Gene Mutations for Human Adaptation in Clinical Isolates of Avian H5N1 Influenza Viruses.
Method: Furthermore, a mouse infection study was performed after observing no increase in progeny vRNA production of the selected viruses carrying mutations compared to previously published studies, and the PB2-D701N mutant virus was excluded from the in vivo mouse infection study although this mutant showed reduced progeny vRNA production in human cells compared to EG/D1 (wt) virus.
Method: In this study, all the mutations introduced into recombinant EG/D1 virus (clade 2.2.1) were naturally detected as single/multiple intra-segment mutations or inter-segment combinations of the mutations in clade 2.2.1 viruses isolated from patients, except artificial mutation PB2-D701N.
Result: In this study, PB2-D701N was included as a reference mutation, although this human adaptation
Detection of reassortant avian influenza A (H11N9) virus in environmental samples from live poultry markets in China.
PMID: 27268229
2016
Infectious diseases of poverty
Table: D701N
Susceptibility and Status of Avian Influenza in Ostriches.
Abstract: Seventeen of 27 (63%) ostrich viruses contained the polymerase basic 2 (PB2) E627K marker, and 2 of the ostrich isolates that lacked E627K contained the compensatory Q591K mutation, whereas a third virus had a D701N mutation.
Amino acid substitutions involved in the adaptation of a novel highly pathogenic H5N2 avian influenza virus in mice.
Result: Several amino acid substitutions including PB2 (Q591K and D701N), polymerase acidic protein (PA) (I554V), HA (S227N), and NP (R351K) have been described in mouse adapted H5N2 AIVs that have increased virulence and enhanced replication kinetics in mice and cell lines.
IV mutation literature information.
PMID: 
2017
Veterinary microbiology
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