Abstract: Here, using reverse genetics, mutations E627K, D701N, and E677G were introduced into the prototype S-OIV A/Netherlands/602/2009, and their effects on virus replication, virulence, and transmission were investigated.
Abstract: Mutations E627K and D701N caused increased reporter gene expression driven by the S-OIV polymerase complex.
Abstract: Mutations E627K and D701N in the PB2 protein have previously been identified as determinants of avian and pandemic influenza virus virulence in mammals.
PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells.
Abstract: We characterized the activity of avian polymerase complexes containing avian-to-human mutations at these conserved PB2 residues and found that, in addition to the E627K mutation, the PB2 mutation T271A enhances polymerase activity in human cells.
Substitution of lysine at 627 position in PB2 protein does not change virulence of the 2009 pandemic H1N1 virus in mice.
Abstract: To explore the potential role of E627K substitution in PB2 in the pandemic (H1N1) 2009 virus, we compared pathogenicity and growth properties between a recombinant virus containing 627K PB2 gene and the parental A/California/4/2009 strain containing 627E.
Discussion: In this study, we demonstrated that the single amino acid substitution of PB2 E627K, in the context of the current influenza pandemic stain, rendered neither increased pathogenecity in mice, nor improved viral replication in MDCK cells under 33-39 C.
Discussion: It was reported that increased virulence in mice caused by the E627K mutation in H5N1 avian influenza virus could be compensated by multiple mutations at other sites of PB2 gene (
Evidence for avian and human host cell factors that affect the activity of influenza virus polymerase.
Abstract: Finally, our results strongly suggest that the well-known adaptative mutation E627K on viral protein PB2 facilitates the ability of a human positive factor to enhance replication of influenza virus in human cells.
V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.
Result: Again, to our surprise, introduction of the mammalian-adaptive PB2-E627K or -D701N mutation into the pandemic RNP significantly attenuated viral replication in mouse lung.
Result: CA09RNP-E627K and CA09RNP-D701N reached approximately 2- and 1-log-lower peak titers than the wild-type CA09RNP virus, respectively (1.1 x 103 and 1.24 x 104 PFU/g versus 2.21 x 105 PFU/g; P = 0.042 and 0.049).
Result: Compared to wild-type CA09RNP, CA09RNP-E627K and CA09RNP-D701N induced similarly mild weight losses.
Result: Compared to wild-type S09RNP, the S09RNP-E627K virus replicated to approximately 1.5-log-greater titers on day 3 (9.9 x 105 versus 5.2 x 104 PFU/g; P
PB2 and hemagglutinin mutations are major determinants of host range and virulence in mouse-adapted influenza A virus.
Abstract: Minigenome transcription assays showed that PB1 and PB2 mutations increased polymerase activity and that the PB2 D701N mutation was comparable in effect to the mammalian adaptive PB2 E627K mutation.
Characterization of an H3N2 triple reassortant influenza virus with a mutation at the receptor binding domain (D190A) that occurred upon virus transmission from turkeys to pigs.
Method: In addition, we generated a virus with a mutation at residue 627 of PB2 gene (Glu627Lys) that has been shown to affect replication and transmission of influenza viruses in different species.
Result: Interestingly, Glu627Lys mutation in the PB2 gene did not affect virus replication in all three cell types (Figure 2), supporting a recent finding which indicated that Glu627Lys substitution in PB2 gene does not increase virulence nor growth rate of pandemic-H1N1 (2009) virus in mice and cell culture.
Result: Virus with a mutation at residue 627 of the PB2 gene (Glu627Lys) was used as control, where such mutation has been shown to affect replication and host range specificity of influenza viruses.
Avian Influenza A virus polymerase association with nucleoprotein, but not polymerase assembly, is impaired in human cells during the course of infection.
Abstract: Sequencing of two isolates recovered from the pigs inoculated with rg-Sw-Ck/PB2 revealed either the D256G or the E627K amino acid substitution in the PB2 proteins of the isolates.
Abstract: The D256G and E627K mutations enhanced viral polymerase activity in the mammalian cells, correlating with replication of virus in pigs.
Transmission of influenza virus in a mammalian host is increased by PB2 amino acids 627K or 627E/701N.
Introduction: A single passage in mice has been reported to be sufficient for an E627K variant to dominate the resultant H5N1 virus population.
Introduction: Similarly to E627K, a change of PB2 amino acid 701 from aspartic acid to asparagine has been implicated in expanding the host range of avian (or avian-like) H5N1 and H7N7 subtype viruses to include mice and humans.
Introduction: This finding has also been confirmed in the context of infected cell cultures: the growth of A/Viet Nam/1204/04 virus (VN1204; H5N1) in mammalian cell lines is improved at 33 C, but not 37 C or 41 C, by the single amino acid change, PB2 E627K.
Discussion: that, with respect to adaptation of an avian virus to a mammalian host, D701N can function
IV mutation literature information.
PMID: 
2010
Journal of virology
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