Key result
The measles virus C protein is a ribonucleocapsid-associated protein that interacts with the phosphoprotein, thereby increasing replication accuracy and processivity of the polymerase complex.
The primary function of the measles virus C protein is to improve polymerase processivity and accuracy by interacting with the P protein on the ribonucleocapsid.
Offers potential measles antiviral target; leaves open clinical translation from animal models.
Replication of negative-strand RNA viruses relies on two components: a helical ribonucleocapsid and an RNA-dependent RNA polymerase composed of a catalytic subunit, the L protein, and a cofactor, the P protein. We show that the measles virus (MeV) C protein is an additional component of the replication complex. We provide evidence that the C protein is recruited to the ribonucleocapsid by the P protein and map the interacting segments of both C and P proteins. We conclude that the primary function of MeV C is to improve polymerase processivity and accuracy, rather than uniquely to antagonize the type I interferon response. Since most viruses of the Paramyxoviridae family express C proteins, their primary function may be conserved.
No takes yet. Share an insight, caveat, or question.
Pfaller et al. (2019) studied Measles virus replication. Measles virus C protein vs. C-deficient measles virus was evaluated on Protein-protein interaction and colocalization. The measles virus C protein is a ribonucleocapsid-associated protein that interacts with the phosphoprotein, thereby increasing replication accuracy and processivity of the polymerase complex.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: