Structure of the measles virus ternary polymerase complex.

ABSTRACT: Measles virus (MeV) is a highly contagious pathogen that causes significant morbidity worldwide. Its polymerase machinery, composed of the large protein (L) and phosphoprotein (P), is crucial for viral replication and transcription, making it a promising target for antiviral drug development. Here we present cryo-electron microscopy structures of two distinct MeV polymerase complexes: L_core-P and L_full-P-C. The L_core-P complex characterizes the N-terminal domain, RNA-dependent RNA polymerase (RdRp), and GDP poly-ribonucleotidyltransferase of the L protein, along with the tetrameric P of varying lengths. The L_full-P-C complex reveals that C protein dimer binds at the cleft between RdRp and the flexible domains of the L protein: the connecting doma

SUBMITTER: Wang D 

PROVIDER: S-EPMC12019284 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature