Abstract: Functions affected include nuclear localization signals and sites of protein and RNA interaction, while others are known determinants of pathogenicity and host specificity such as the viral polymerase PB2 E627K substitution.
Single mutation at the amino acid position 627 of PB2 that leads to increased virulence of an H5N1 avian influenza virus during adaptation in mice can be compensated by multiple mutations at other sites of PB2.
Abstract: Taken together, the results suggest that mutations at multiple sites of PB2 contributed to the virulence and adaptation in mice, and the E627K mutation of PB2 is not an indispensable determinant in PB2 for mammalian adaptation by H5N1 avian influenza virus.
Interaction of polymerase subunit PB2 and NP with importin alpha1 is a determinant of host range of influenza A virus.
Introduction: PB2 mutation D701N has also been implicated in the adaptation of H5N1 viruses to mammalian hosts but other mutations may be involved, too, notably PB2 mutation E627K.
Mutations in influenza A virus (H5N1) and possible limited spread, Turkey, 2006.
Conclusion: The Q447L and E627K mutations in FK and MAK virus isolates indicate a common origin of viruses in the 2 siblings.
Method: Enhanced pathogenic potential of all avian and human influenza virus isolates from the second outbreak was shown by mutation E627K in the PB2 region.
Table: E627K
Host determinant residue lysine 627 lies on the surface of a discrete, folded domain of influenza virus polymerase PB2 subunit.
Discussion: From an analysis of H5N1 viruses isolated from infected humans in Vietnam it was observed that in 5/8 fatal and 3/4 non-fatal cases the E627K mutation had occurred.
Discussion: Interestingly, in 3/4 cases retaining Glu627, but none of those with E627K, the D701N mutation was also found, leading to the suggestion that the latter mutation may compensate for the lack of change at position 627.
The human H5N1 influenza A virus polymerase complex is active in vitro over a broad range of temperatures, in contrast to the WSN complex, and this property can be attributed to the PB2 subunit.
PMID: 19008377
2008
The Journal of general virology
Abstract: The E627K mutation in the avian PB2 was not required for this effect.
Method: The E627K mutation was introduced by site-directed mutagenesis (Quick-Change mutagenesis kit, Stratagene).
Result: 5b and d, respectively) and found, that an E627K mutation slightly shifted the temperature optimum from 37 C to 39 C.
Result: Interestingly, in both assays an E627K mutation in the avian PB2 resulted in a slight increase in activity.
Discussion: The E627K mutation in the avian PB2 led to only a slight increase in thermotolerance.
Adaptation of an H7N7 equine influenza A virus in mice.
PMID: 17251573
2007
The Journal of general virology
Abstract: It was found that the PB2-E627K substitution in this equine virus contributed to increased viral protein expression and virus replication in mouse cells and enhanced brain invasiveness in mice.
Abstract: Of these mutations, the Glu-to-Lys substitution at position 627 of PB2 (PB2-E627K) increased virulence appreciably.
Abstract: These results demonstrate that the importance of the PB2-E627K substitution for mouse adaptation, which was identified previously in human H5N1 isolates, extends to equine influenza A virus.
An avian influenza vaccine for humans targeting the polymerase B2 protein inside the capsid instead of hemagglutinin or neuramidase on the virus surface.
Abstract: Consequently, a publicly available database at the National Center for Biotechnology Information (NCBI) website, and the SYFPEITHI online computer algorithm, were used to generate a hypothesis about a peptide-based vaccine targeted at the E627K mutation in PB2 of the avian influenza virus.
Abstract: However, a recent study has revealed that the 1918 flu virus, like the H5N1 avian flu virus, has an E627K mutation in its polymerase B2 component, which is located inside the virus capsid.
Abstract: It seems reasonable to believe that the constancy, over more than 80 years, of the E627K mutation could be exploited to begin developing a vaccine now, rather than waiting for new mutations.
PB2 amino acid at position 627 affects replicative efficiency, but not cell tropism, of Hong Kong H5N1 influenza A viruses in mice.
Abstract: A single amino acid substitution, from glutamic acid to lysine at position 627 of the PB2 protein, converts a nonlethal H5N1 influenza A virus isolated from a human to a lethal virus in mice.
IV mutation literature information.
PMID: 
2009
Veterinary microbiology
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