2026-03-10T18:42:46Z https://tokushima-u.repo.nii.ac.jp/oai

oai:tokushima-u.repo.nii.ac.jp:02003255 2025-04-28T06:42:49Z 1713853213384:1713853295607

Mechanism of a Mutation in Non-Structural Protein 1 Inducing High Pathogenicity of Avian Influenza Virus H5N1 Mechanism of a Mutation in Non-Structural Protein 1 Including High Pathogenicity of Avian Influenza Virus H5N1 加藤, 有介 カトウ, ユウスケ Kato, Yusuke 加藤 カトウ Kato 有介 ユウスケ Yusuke 00175564 福井, 清 フクイ, キヨシ Fukui, Kiyoshi 福井 フクイ Fukui 清 キヨシ Kiyoshi 鈴木, 和男 スズキ, カズオ Suzuki, Kazuo open access avian Influenza non-structural protein 1 structure modeling cytokine storm double-stranded RNA interaction Avian influenza H5N1 has shown high mortality rate in human. Non-structural protein 1 (NS1) is a virulence factor of H5N1. Mutation at the 42nd residue within the RNA-binding domain (RBD) of NS1 dramatically changes the degree of pathogenicity of H5N1 in mice. We here studied the impact of this mutation on the function of RBD, and found that RBD with serine at the 42th residue binds doublestranded RNA (dsRNA), whereas that with proline at the 42th residue does not. Analysis of structural models of the RBD proteins with S42 and P42 suggested remarkable difference in the structure of the dsRNA-binding interface, whereas structural analysis by analytical gel filtration and CD measurements did not indicate difference between those RBD proteins. Our results suggest that the single amino acid replacement induces a minor, but global structural change leading to the loss of function of NS1 thereby the change in the degree of pathogenicity. 2016 eng journal article AM 311902 https://tokushima-u.repo.nii.ac.jp/records/2003255 https://doi.org/10.2174/0929866523666160204124406 10.2174/0929866523666160204124406 09298665 AA1102463X Protein and Peptide Letters 23 4 372 378 https://tokushima-u.repo.nii.ac.jp/record/2003255/files/LID201704072001.pdf application/pdf 2.05 MB 2017-04-07