nihao guest [ sign in / register ]
2019-9-16 11:04:05

Teo SHC, Wu JP, Mok CK, Tan YJ. A NS1-Binding Monoclonal Antibody Interacts with Two Residues that are Highly Conserved in Seasonal as well as Newly-Emerged Influenza A Virus. Pathog Dis. 2019 Mar 6
submited by kickingbird at Mar, 8, 2019 14:11 PM from Pathog Dis. 2019 Mar 6

The non-structural protein 1 (NS1) of influenza A virus (IAV) is a multifunctional protein that antagonizes host antiviral responses, modulating virus pathogenesis. As such, it serves as a good target for research and diagnostic assay development. In this study, we have generated a novel monoclonal antibody (mAb) 19H9 and epitope mapping revealed that two residues, P85 and Y89, of NS1 are essential for interacting with this mAb. Furthermore, residues P85 and Y89 are found to be highly conserved across different IAV subtypes, namely seasonal H1N1 and H3N2, as well as the highly pathogenic H5N1 and H5N6 avian strains. Indeed, mAb 19H9 exhibits broad cross-reactivity with IAV strains of different subtypes. The binding of mAb 19H9 to residue Y89 was further confirmed by the abrogation of interaction between NS1 and p85β. Additionally, mAb 19H9 also detected NS1 proteins expressed in IAV-infected cells, showing NS1 intracellular localization in the cytoplasm and nucleolus. To our knowledge, mAb 19H9 is the first murine mAb to bind at the juxtaposition between the N-terminal RNA-binding domain and C-terminal effector domain of NS1. It could serve as a useful research tool for studying the conformational plasticity and dynamic changes in NS1.

See Also:

Latest articles in those days:

[Go Top]    [Close Window]

Related Pages:
Learn about the flu news, articles, events and more
Subscribe to the weekly F.I.C newsletter!


Site map  |   Contact us  |  Term of use  |  FAQs
Copyright ©www.flu.org.cn. 2004-2019. All Rights Reserved. Powered by FIC 4.0.1