Priming and realignment by the influenza a virus RNA-Dependent RNA Polymerase is dependent on the length of the host primers and the extent of base pairing to viral RNA.
substitutions in HA (Asp225Gly or Gln226Arg) and compensatory mutation decreasing the charge of HA (Lys123Asn Lys157Asn Gly158Glu Asn159Asp or Lys212Met) altered viral receptor-binding specificity and restored the functional balance between HA and NA; (2) Phe35Leu substitution in the PA protein increased viral polymerase activity.
A recombinant pandemic H1N1 virus containing PA PA-X and NS1 genes from currently circulating viruses is fitter in replication in cultured cells and in mice and is slightly more pathogenic than the original ancestor pandemic H1N1 virus.
Computational analysis of the effect of polymerase acidic gene mutation F35L in the 2009 pandemic influenza A (H1N1) virus on binding aspects of mononucleotides in the endonuclease domain has been presented.
The ts-mutations in PB1 PB2 and PA genes are mostly involved in the modulation of the humoral immunity but also have a moderate effect on the cellular adaptive immune response.
The human (H1N1) and avian (H7N9) strain PA-C-terminal domain proteins exhibit the same global topology as other strains in the absence of PB1 but differ extensively in the PB1 binding pocket.
These results indicate that the PB2 PA NP and M segments play a more important role than the remaining four viral RNAs during the genome-packaging process.
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