Structural and functional insights into calmodulin-mediated lipid binding and proteolytic cleavage of the M-PMV matrix protein.

ABSTRACT: The matrix (MA) domain of the Mason-Pfizer monkey virus (M-PMV) Gag polyprotein plays a central role in retroviral assembly and trafficking, coordinating membrane association and proteolytic maturation. Unlike HIV-1, M-PMV assembles immature particles in the cytoplasm prior to plasma membrane targeting, but the molecular mechanisms governing this process remain poorly understood. Here, we identify calmodulin (CaM) as a calcium-dependent modulator of MA structural dynamics. Using a combination of biophysical and biochemical methods, we demonstrate that CaM directly interacts with myristoylated MA, promoting its oligomerization and enhancing its cleavage by the viral protease. In-depth characterization of MA-CaM complex by protein cross-linking mass spectrometry, hydrogen/deuterium exchange

SUBMITTER: Buresova K 

PROVIDER: S-EPMC12858339 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature