Oligomerization and Cell Egress Controlled by Two Microdomains of Canine Distemper Virus Matrix Protein.

ABSTRACT: The multimeric matrix (M) protein of clinically relevant paramyxoviruses orchestrates assembly and budding activity of viral particles at the plasma membrane (PM). We identified within the canine distemper virus (CDV) M protein two microdomains, potentially assuming α-helix structures, which are essential for membrane budding activity. Remarkably, while two rationally designed microdomain M mutants (E89R, microdomain 1 and L239D, microdomain 2) preserved proper folding, dimerization, interaction with the nucleocapsid protein, localization at and deformation of the PM, the virus-like particle formation, as well as production of infectious virions (as monitored using a membrane budding-complementation system), were, in sharp contrast, strongly impaired. Of major importance, raster image corr

SUBMITTER: Gast M 

PROVIDER: S-EPMC8546710 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature