Abstract: Here, we constructed recombinant viruses by introducing E627K or D701N into the PB2 gene in the genetic background of A/Canine/Guangdong/02/2011H3N2 using a reverse-genetic system.
Abstract: However, how the E627K and D701N substitutions in the PB2 subunit might affect the virulence of CIV H3N2 is unclear.
Abstract: Previous studies have reported that the E627K and D701N substitutions in the PB2 subunit enhanced viral pathogenicity to mammals in various influenza viruses.
Abstract: The results showed that the E627K or D701N substitutions in the PB
Dynamic Variation and Reversion in the Signature Amino Acids of H7N9 Virus During Human Infection.
PMID: 29688498
2018
The Journal of infectious diseases
Abstract: Neuraminidase (NA) R292K, basic polymerase 2 (PB2) E627K, and D701N were the 3 most dynamic mutations.
Abstract: Dual D701N and E627K mutations emerged but failed to achieve predominance in any of the samples.
Table: D701N
Discussion: Although dual E627K and D701N mutations in the PB2 segment confer higher H7N9 viral polymerase activity and improve viral replication in mammalian cells over a single E627K or D701N mutation, this dual mutation did not achieve predominance i
Amino Acid Substitutions HA A150V, PA A343T, and PB2 E627K Increase the Virulence of H5N6 Influenza Virus in Mice.
Introduction: For example, polymerase acidic (PA) R443 K, PA-K356R, polymerase basic 2 protein (PB2) E627K, PB2 D701N, and polymerase basic protein 1 (PB1) D622G) are all associated with replication and host tropism.
Human Clade 2.3.4.4 A/H5N6 Influenza Virus Lacks Mammalian Adaptation Markers and Does Not Transmit via the Airborne Route between Ferrets.
Discussion: Out of the 16 A/H5N6 human isolates, seven isolates carry the PB2-E627K, and one isolate, A/Sichuan/26221/2014, carries the PB2-D701N substitution, which has also been associated with increased replication and transmission in mammalian hosts.
Emergence and Adaptation of a Novel Highly Pathogenic H7N9 Influenza Virus in Birds and Humans from a 2013 Human-Infecting Low-Pathogenic Ancestor.
Abstract: Notably, human-origin viruses were more pathogenic in mice than avian viruses, and the mutations in the PB2 gene associated with adaptation to mammals (E627K, A588V, and D701N) were identified by next-generation sequencing (NGS) and Sanger sequencing of the isolates from infected mice.
Rapid acquisition adaptive amino acid substitutions involved in the virulence enhancement of an H1N2 avian influenza virus in mice.
Abstract: The MVV mutations caused no weight loss in mice, but they did allow replication in infected lungs, and the viruses acquired fatal mammalian pathogenic mutations such as Q591R/K, E627K, or D701N in the infected lungs.
Result: Cloned amplicons encoding amino acid residues 590-701 were sequenced, and well-known mammalian pathogenic mutations such as Q591R/K, E627K, and D701N were identified in four out of five lungs.
Result: Surprisingly, at least half of the quasi-species of three mice possessed mammalian pathogenic mutations (Q591K, E627K, or D701N), and double mutations [E627K (10/10) and
Multiple amino acid substitutions involved in the virulence enhancement of an H3N2 avian influenza A virus isolated from wild waterfowl in mice.
Abstract: Genomic analysis revealed mutations in the PB2 (E192K and D701N), PB1 (F269S, I475V, and L598P), HA (V242E), NA (G170R), and M1 (M192V) proteins.
Enhanced pathogenicity and neurotropism of mouse-adapted H10N7 influenza virus are mediated by novel PB2 and NA mutations.
PMID: 28597818
2017
The Journal of general virology
Abstract: Sequencing showed the absence of the widely recognized mammalian adaptation markers of E627K and D701N in PB2 in the mouse-adapted strain; instead, five amino acid mutations were identified: E158G and M631L in PB2; G218E in haemagglutinin (H3 numbering); and K110E and S453I in neuraminidase (NA).
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-
IV mutation literature information.
PMID: 
2018
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