Structure of the measles virus ternary polymerase complex DOI Creative Commons

Dong Wang,

Ge Yang, Bin Liu

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: April 23, 2025

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), crucial for viral replication transcription, making it promising target antiviral drug development. Here we present cryo-electron microscopy structures two distinct MeV complexes: Lcore-P Lfull-P-C. The complex characterizes N-terminal domain, RNA-dependent RNA (RdRp), GDP poly-ribonucleotidyltransferase L protein, along with tetrameric P varying lengths. Lfull-P-C reveals C dimer binds at cleft between RdRp flexible domains protein: connecting methyltransferase C-terminal domain. This interaction results in visualization these creates an extended channel, remodeling putative nascent replicated exit potentially regulating synthesis processivity. Our findings reveal architecture molecular details complexes, providing new insights into their mechanisms suggesting potential intervention targets therapy.

Language: Английский

Structure of the measles virus ternary polymerase complex DOI Creative Commons

Dong Wang,

Ge Yang, Bin Liu

et al.

Nature Communications, Journal Year: 2025, Volume and Issue: 16(1)

Published: April 23, 2025

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), crucial for viral replication transcription, making it promising target antiviral drug development. Here we present cryo-electron microscopy structures two distinct MeV complexes: Lcore-P Lfull-P-C. The complex characterizes N-terminal domain, RNA-dependent RNA (RdRp), GDP poly-ribonucleotidyltransferase L protein, along with tetrameric P varying lengths. Lfull-P-C reveals C dimer binds at cleft between RdRp flexible domains protein: connecting methyltransferase C-terminal domain. This interaction results in visualization these creates an extended channel, remodeling putative nascent replicated exit potentially regulating synthesis processivity. Our findings reveal architecture molecular details complexes, providing new insights into their mechanisms suggesting potential intervention targets therapy.

Language: Английский

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