Respiratory syncytial virus transcription antitermination factor M2-1 (M2-1)

The Respiratory syncytial virus (RSV) transcription antitermination factor M2-1 is an essential structural protein that functions as a processivity factor for the viral RNA-dependent RNA polymerase (RdRp) complex (UniProt P04545). It plays a critical role in the viral life cycle by preventing the premature termination of transcription at gene junctions, thereby ensuring the synthesis of full-length, polyadenylated messenger RNAs (PubMed: 25410397). M2-1 exists as a tetramer and contains a distinct zinc-finger domain and an RNA-binding domain, both of which are necessary for its recruitment to the transcription complex via interaction with the viral phosphoprotein (P) (PubMed: 21835792). In clinical contexts, RSV is a major cause of severe lower respiratory tract infections, such as bronchiolitis and pneumonia, particularly in infants, the elderly, and immunocompromised individuals (CDC). Because M2-1 is highly conserved within the Pneumoviridae family and has no human homolog, it represents a promising target for the development of specific antiviral therapies (PubMed: 28490585). Current therapeutic strategies focus on small-molecule inhibitors designed to disrupt the M2-1/P protein-protein interaction or interfere with M2-1's ability to bind RNA, effectively halting viral replication (PubMed: 30115704).

Other names

M2-1 proteinTranscription antitermination factorRSV M2-1Protein M2-1

Inhibition of viral transcription processivity by disrupting the interaction between the M2-1 protein and the viral phosphoprotein (P) or by blocking M2-1 RNA binding.