Experimental Evidence of Intrinsic Disorder and Amyloid Formation by the Henipavirus W Proteins.

ABSTRACT: Henipaviruses are severe human pathogens within the Paramyxoviridae family. Beyond the P protein, the Henipavirus P gene also encodes the V and W proteins which share with P their N-terminal, intrinsically disordered domain (NTD) and possess a unique C-terminal domain. Henipavirus W proteins antagonize interferon (IFN) signaling through NTD-mediated binding to STAT1 and STAT4, and prevent type I IFN expression and production of chemokines. Structural and molecular information on Henipavirus W proteins is lacking. By combining various bioinformatic approaches, we herein show that the Henipaviruses W proteins are predicted to be prevalently disordered and yet to contain short order-prone segments. Using limited proteolysis, differential scanning fluorimetry

SUBMITTER: Pesce G 

PROVIDER: S-EPMC8780864 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature