PB2 E627K or D701N substitution does not change the virulence of canine influenza virus H3N2 in mice and dogs.
PMID: 26074198
2015
European journal of cell biology
Abstract: To throw light on the role of the NLSs of NP and PB2 in nuclear transport, we have analysed the effect of mutation D701N, responsible for the exposure of the NLS domain of PB2, on the intracellular localisation of vRNPs.
Molecular docking of potential inhibitors for influenza H7N9.
PMID: 25861376
2015
Computational and mathematical methods in medicine
Introduction: Previously, it was observed that the Asp701Asn mutation in PB2 and the Ser31Asn mutation in hemagglutinin increased the adaptability to mammals, and the Ser31Asn mutation of M2 contributed at least partly to the resistance of antivirus drugs including amantadine and rimantadine.
Analysis of the full-length genome of a novel strain of the H7N9 avian influenza virus.
PMID: 24940441
2014
Experimental and therapeutic medicine
Result: However, only one virus harbored the D701N mutation.
Result: No E627K and D701N mutations were detected in the A/Changsha/2/2013 PB2 protein (Table II).
Discussion: Although no E627K and D701N mutations were detected in the PB2 protein of A/Changsha/2/2013, the E627K mutation and D701N mutation occurred in eight human H7N9 virus strains and one human H7N9 virus strain among the 51 new H7N9 viruses, respectively.
Discussion: However avian and environmental H7N9 viruses had no E627K and D701N mutations.
Discussion: The E627K and
Amino acid substitutions in polymerase basic protein 2 gene contribute to the pathogenicity of the novel A/H7N9 influenza virus in mammalian hosts.
Abstract: Only five amino acid mutations in four viral proteins (HA-S227N, PB2-Q591K, PB2-D701N, PA-I554V and NP-R351K) of HB10-MA virus were found when compared with those of HB10, indicating that they may be responsible for the adaptation of the novel reassortant H5N2 avian influenza virus in mice with increased virulence and replication efficiency.
The K526R substitution in viral protein PB2 enhances the effects of E627K on influenza virus replication.
Introduction: PB2 D701N and Q591K substitutions were also found to support H5N1 virus replication in mammalian hosts.
Introduction: While about 50% of H5N1 human isolates contain known PB2 adaptation markers, mainly E627K with some D701N and a few instances of 591K, as described above, the other half of human infections are not associated with known adaptation markers.
PB2 E627K or D701N substitution does not change the virulence of canine influenza virus H3N2 in mice and dogs.
Abstract: Interestingly, virus isolates from co-caged guinea pigs had the D701N mutation in the PB2 protein.
Discussion: In our study, the D701N mutation in PB2 protein did not enhance the virus's transmission ability among guinea pigs which suggest other genes may affect virus's ability to transmission among the guinea pigs.
Discussion: Interestingly, the viruses isolated from the co-caged guinea pigs had a D701N mutation in the PB2 protein.
Discussion: found that when PB2 627 holds a glutamic acid residue, the D701N mutation not only improves viral growth in mammalian cells but enhances transmission of both human influenza viruses and AIVs among guinea pigs.
Discussion: reported t
Human H7N9 avian influenza virus infection: a review and pandemic risk assessment.
Abstract: Infection in Ratitae species may lead to the selection of PB2-E627K and PB2-D701N mutants and the conversion of nH7N9 to a highly pathogenic avian influenza virus.
Abstract: nH7N9 isolated from humans contains features related to adaptation to humans, including a Q226L mutation in the hemagglutinin cleavage site and E627K and D701N mutations in the PB2 protein.
Introduction: Because influenza infection of ostrich and emu can lead to the selection of PB2-E267K and PB2-D701N<
Asparagine substitution at PB2 residue 701 enhances the replication, pathogenicity, and transmission of the 2009 pandemic H1N1 influenza A virus.
Abstract: In addition, compared to the NY1682-WT virus, the NY1682-D701N mutant virus induced less IFN-lambda and replicated to a higher titer in primary human alveolar epithelial cells.
Abstract: Mini-genome replication assay, in vitro replication characteristics in cell lines, and analysis in the mouse and ferret models demonstrated that PB2-D701N increased virus replication rates and resulted in more severe pathogenicity in mice and more efficient transmission in ferrets.
Abstract: The 2009/2010 pandemic influenza virus (H1N1pdm) contains an avian-lineage PB2 gene that lacks E627K and D701N substitutions important in the pathogenesis and transmission of avian-origin viruses in humans or other mammals.
IV mutation literature information.
PMID: 
2015
European journal of cell biology
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