Rabies virus phosphoprotein (P), matrix protein (M), and RNA-directed RNA polymerase (L) (RABV P-M-L)

The Rabies virus phosphoprotein (P), matrix protein (M), and RNA-directed RNA polymerase (L) are essential components of the Rabies virus (RABV) life cycle, collectively facilitating viral replication, transcription, and assembly. The L protein is the catalytic core of the RNA-dependent RNA polymerase (RdRp) complex, performing all enzymatic activities required for RNA synthesis, capping, and polyadenylation (PMID: 28724771). The P protein serves as a vital cofactor for the L protein and a chaperone for the nucleoprotein, while also acting as a major interferon antagonist that suppresses the host immune response (PMID: 16140868). The M protein is a multifunctional structural protein that regulates the balance between viral transcription and replication and mediates the budding of progeny virions from the host cell membrane (PMID: 11832466). Because these proteins are indispensable for viral survival and lack human homologs, they are prime targets for antiviral drug development. Experimental drugs such as Favipiravir target the L protein's polymerase activity to inhibit viral progression (PMID: 24954874). Therapeutic challenges include the rapid progression of the disease and the difficulty of delivering inhibitors across the blood-brain barrier to the infected neurons (PMID: 30634450).

Other names

Rabies virus P proteinRabies virus M proteinRabies virus L proteinRabies virus replication complexRABV P-M-L complexRabies virus ribonucleoprotein complex components

Inhibition of the RNA-dependent RNA polymerase (RdRp) complex, leading to the termination of viral RNA synthesis or the induction of lethal mutations in the viral genome (PMID: 24954874).