Abstract: During a large influenza A(H7N7) virus outbreak in the Netherlands in 2003, the A(H7N7) virus isolated from a fatal human case contained the PB2 E627K mutation as well as a hemagglutinin (HA) K416R mutation.
Abstract: In both the avian influenza A(H5N1) and the recently emerging avian influenza A(H7N9) viruses, the polymerase basic 2 protein (PB2) E627K mutation appears to be of key importance for human adaptation.
Abstract: In the human samples, the PB2 E627K mutation was identified with increasing frequency during infection.
Abstract: Our results strongly suggest that human adaptation marker
V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.
PMID: 24394699
2014
The Journal of general virology
Abstract: In this study, we demonstrate that the PB2 E627K mutation, which occurs in over 70 % of the H7N9 patient isolates, promotes the replication of H7N9 virus by enhancing PB2 polymerase activity and enhances virulence in mice.
Abstract: Our results show the PB2 E627K mutation has played an important role in this H7N9 influenza outbreak and in the pathogenicity of the H7N9 virus.
Amino acid substitutions in polymerase basic protein 2 gene contribute to the pathogenicity of the novel A/H7N9 influenza virus in mammalian hosts.
Abstract: In this study, we determined the contribution of PB2-E627K in H7N9 virus to its pathogenicity in mammalian hosts.
Abstract: Since many human (but not avian) H7N9 virus isolates have an amino acid substitution at position E627K in the polymerase basic protein 2 (PB2) gene, we investigated the role of this and other functionally related mutations for polymerase activity in vitro, virus replication competence, and pathogenicity in the mouse model.
Abstract: We found that E627K and functionally related mutations are associated with increased polymerase activity, increased viral replication competence, and increased disease severity in mice.
Unique reassortant of influenza A(H7N9) virus associated with severe disease emerging in Hong Kong.
Result: In the PB2 polymerase subunit, A/Hong Kong/470129/2013 contains L89V and E627K substitutions which are associated with enhanced viral polymerase activity in mammalian cells.
Complex reassortment of polymerase genes in Asian influenza A virus H7 and H9 subtypes.
PMID: 24632455
2014
Infection, genetics and evolution
Abstract: Furthermore, the most recent reassortments occurred multiply on the polymerase genes of the newly emerging H7N9 isolated from human in South China, evolving E627K mutation in PB2 independently.
Analysis of the full-length genome of a novel strain of the H7N9 avian influenza virus.
PMID: 24940441
2014
Experimental and therapeutic medicine
Result: No E627K and D701N mutations were detected in the A/Changsha/2/2013 PB2 protein (Table II).
Result: The PB2 gene of eight viruses among 51 new H7N9 viruses harbored the E627K mutation.
Discu
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.
Influenza A virus polymerase is a site for adaptive changes during experimental evolution in bat cells.
Abstract: Adaptation of an avian virus-like virus resulted in the canonical PB2 E627K mutation that is required for efficient replication in other mammals.
V292I mutation in PB2 polymerase induces increased effects of E627K on influenza H7N9 virus replication in cells.
Abstract: Our results demonstrate that PB2-E627K and PA-T97I enhance the ability of H6N1 virus to replicate and cause disease in mammals.
Abstract: Polymerase complexes possessing either PB2-E627K, PA-T97I, and PB2-E627K/PA-T97I displayed higher virus polymerase activity when compared to the wild-type virus, which may account for the increased replication kinetics and enhanced virulence of variant viruses.
Abstract: We found that the recombinant H6N1 viruses possessing both the PA-T97I and
Mutations to PB2 and NP proteins of an avian influenza virus combine to confer efficient growth in primary human respiratory cells.
Abstract: In addition, minimal combinations of three (PB2 Q236H, E627K, and NP N309K) or two (PB2 Q591K and NP S50G) mutations were sufficient to recapitulate the efficient growth in HTBE cells of dk/AB/76 viruses isolated after 10 passages in this substrate.
Abstract: The results indicate that coupling of the mammalian-adaptive mutation PB2 E627K or Q591K to selected mutations in NP further augments the growth of the corresponding viruses.
A combination of HA and PA mutations enhances virulence in a mouse-adapted H6N6 influenza A virus.
IV mutation literature information.
PMID: 
2014
Journal of virology
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