ID 110030
Title Alternative
Mechanism of a Mutation in Non-Structural Protein 1 Including High Pathogenicity of Avian Influenza Virus H5N1
Author
Kato, Yusuke S. The Institute for Enzyme Research, Tokushima University|Institute for Health Sciences, Tokushima Bunri University Tokushima University Educator and Researcher Directory KAKEN Search Researchers
Suzuki, Kazuo Asia International Institute of Infectious Disease Control, and Department of Health Protection, Graduate School of Medicine, Teikyo University
Keywords
avian Influenza
non-structural protein 1
structure modeling
cytokine storm
double-stranded RNA
interaction
Content Type
Journal Article
Description
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.
Journal Title
Protein and Peptide Letters
ISSN
09298665
NCID
AA1102463X
Volume
23
Issue
4
Start Page
372
End Page
378
Sort Key
372
Published Date
2016
Remark
Running Title : NS1 Mechanism of High Pathogenicity of H5N1
The published manuscript is available at EurekaSelect via http://www.eurekaselect.com/openurl/content.php?genre=article&doi=10.2174/0929866523666160204124406.
EDB ID
Published Source
Protein and Peptide Letters (2016) Vol.23 Issue4 p.372-378
URL ( Publisher's Version )
FullText File
language
eng
TextVersion
Author
departments
Institute of Advanced Medical Sciences