Deep sequencing reveals the viral adaptation process of environment-derived H10N8 in mice.
PMID: 26477933
2016
Infection, genetics and evolution
Abstract: Using Illumina high-throughput data, we detected the gradual mutations of F277S, C278Q, F611S and L653P in the polymerase acidic (PA) protein, and of L207V and E627K in the PB2 protein during adaptation.
Species difference in ANP32A underlies influenza A virus polymerase host restriction.
Abstract: Substitutions, such as PB2(E627K), were rapidly selected upon infection of humans with avian H5N1 or H7N9 influenza viruses, adapting the viral polymerase for the shorter mammalian ANP32A.
Introduction: Acquisition of host-adapting mutations, such as PB2 E627K, enables polymerase activity to be supported by the shorter ANP32 proteins typical of mammalian hosts.
Introduction: Each RH clone was screened for the ability to support activity of a H5N1 avian influenza virus polymerase (A/turkey/England/50-92/91 virus (50-92)) compared with its human
Method: The PB2 E627K substitution was made to 50-92, Ty05 (K627E) by overlapping PCR of the PB2 plasmid as previously described .
PB2-588 V promotes the mammalian adaptation of H10N8, H7N9 and H9N2 avian influenza viruses.
Introduction: One well-characterized mutation in PB2 is the glutamate change to lysine at position 627 (E627K) that results in efficient virus replication in mammalian cells and enhanced virulence in mammals.
Result: Consistent with the results of polymerase activity, both G1-PB2 588V and G1-PB2 627K mutant viruses replicated more efficiently than the wild type parental G1 virus in both MDCK and HEK293T cells, but did not grow to the same high titers as the double mutant G1-PB2&nbs
Result: although it did not result in a markedly increased virulence when compared to introduction of substitution E627K or A588V/E627K into the PB2.
Genomic Signatures for Avian H7N9 Viruses Adapting to Humans.
Conclusion: Numerous human-isolated avian influenza A viruses exhibit PB2 627K, which is a human-specific signature, and strong biological evidence indicates that an E627K mutation promotes avian viral replication in mammals.
Conclusion: We used a reporter assay to test all of these substitutions and showed that either Q591K, M535L, or D701N mutation incr
Introduction: Moreover, the replication-promoting PB2 E627K mutation dominated the H7N9 patient isolates.
Introduction: Three genetic substitutions, PB2 E627K, D701N, and Q591R, have been reported to affect host cell tropism.
Amino acid substitutions occurring during adaptation of an emergent H5N6 avian influenza virus to mammals.
Abstract: We provide evidence that the mutations HA A150V, NA R143K and G147E, PB2 E627K, and PA A343T may be important for adaptation of H5N6 AIVs to mammals.
Multiple Natural Substitutions in Avian Influenza A Virus PB2 Facilitate Efficient Replication in Human Cells.
Abstract: Although substitutions like E627K in the PB2 polymerase subunit can facilitate polymerase activity to allow replication in mammals, many human H5N1 and H7N9 viruses lack this adaptive substitution.
Novel Polymerase Gene Mutations for Human Adaptation in Clinical Isolates of Avian H5N1 Influenza Viruses.
Abstract: A major determinant in the change of the avian influenza virus host range to humans is the E627K substitution in the PB2 polymerase protein.
Abstract: However, the polymerase activity of avian influenza viruses with a single PB2-E627K mutation is still lower than that of seasonal human influenza viruses, implying that avian viruses require polymerase mutations in addition to PB2-627K for human adaptation.
Introduction: The
Introduction: The most well-known human adaptation polymerase mutation is the PB2-E627K substitution, which is present in most seasonal human viruses, except for the 2009 pandemic H1N1 virus, and is also in some H5N1 and H7N9 human isolates and one H7N7 human isolate.
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: E627K
Susceptibility and Status of Avian Influenza in Ostriches.
Abstract: Ostriches maintain a low upper- to midtracheal temperature as part of their adaptive physiology for desert survival, which may explain the selection in ratites for E627K or its compensatory mutations-markers that facilitate AIV replication at lower temperatures.
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.
Prevailing PA Mutation K356R in Avian Influenza H9N2 Virus Increases Mammalian Replication and Pathogenicity.
Abstract: In addition, combined mutation of PA-K356R and PB2-E627K, a well-known mammalian adaptive marker, in the H9N2 virus showed further cooperative increases in virus production and severity of infection in vitro and in vivo In summary, PA-K356R behaves as a novel mammalian tropism mutation, which, along with other mutations such as PB2-E627K, might render avian H9N2 viruses adapted for human infection.
Abstract: We found that PA-356R in H9N2 viruses causes significant increases in virus replication and severity of infection in human cells and mice and that PA-K356R cooperates with the
ViMRT
IV mutation literature information.
PMID: 
2016
Infection, genetics and evolution
