Bhoye D, Cherian SS. Computational analysis of the effect of polymerase acidic (PA) gene mutation F35L in the 2009 pandemic influenza A (H1N1) virus on binding aspects of mononucleotides in the endonuclease domain. Arch Virol 2017 Dec 22
An F35L mutation in the N-terminal domain of the polymerase acidic protein (PA-Nter), which contains the active site of the endonuclease, has been reported to result in higher polymerase activity in mouse-adapted strains of the 2009 pandemic influenza A H1N1 virus. We modeled wild and mutant complexes of uridine 5´-monophosphate (UMP) as the endonuclease substrate and performed molecular dynamics simulations. The results demonstrated that the F35L mutation could result in a changed orientation of a helix containing active site residues and improve the ligand affinity in the mutant strain. This study suggests a molecular mechanism of enhanced polymerase activity.
See Also:
Latest articles in those days:
- Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation 1 days ago
- Risk assessment of a highly pathogenic H5N1 influenza virus from mink 1 days ago
- Detection of clade 2.3.4.4b highly pathogenic H5N1 influenza virus in New York City 1 days ago
- Sequence-based epitope mapping of high pathogenicity avian influenza H5 clade 2.3.4.4b in Latin America 2 days ago
- Guanylate-binding protein 1 inhibits inflammatory factors produced by H5N1 virus through Its GTPase activity 2 days ago
[Go Top] [Close Window]