Nipah Virus V Protein Binding Alters MDA5 Helicase Folding Dynamics.

ABSTRACT: Nipah virus (NiV) is an emerging and deadly zoonotic paramyxovirus that is responsible for periodic epidemics of acute respiratory illness and encephalitis in humans. Previous studies have shown that the NiV V protein antagonizes host antiviral immunity, but the molecular mechanism is incompletely understood. To address this gap, we biochemically characterized NiV V binding to the host pattern recognition receptor MDA5. We find that the C-terminal domain of NiV V (V_CTD) is sufficient to bind the MDA5_SF2 domain when recombinantly co-expressed in bacteria. Analysis by hydrogen-deuterium exchange mass spectrometry (HDX-MS) studies revealed that NiV V_CTD is conformationally dynamic, and binding to MDA5 reduces the dynamics of V_CTD. Our results also s

SUBMITTER: Wagner ND 

PROVIDER: S-EPMC8762660 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature