A Coronaviral Pore-Replicase Complex Drives RNA Synthesis in Double Membrane Vesicles DOI Creative Commons

A. Chen,

Ana‐Mihaela Lupan, Rui Tong Quek

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: June 18, 2024

Abstract Coronavirus-infected cells contain double-membrane vesicles (DMVs) that are key for viral RNA replication and transcription, perforated by hexameric pores connecting the vesicular lumen to cytoplasm. How form traverse two membranes, how DMVs organize synthesis, is unknown. Using structure prediction functional assays, we show non-structural membrane protein nsp4 DMV pore organizer, spanning double forming most of lining. Nsp4 interacts with nsp3 on cytoplasmic side replicase inside DMV. Newly synthesized mRNAs exit into cytoplasm, passing through a narrow ring conserved residues. Steric constraints imposed predict modified nucleobases block mRNA transit, broad spectrum anti-coronaviral activity.

Language: Английский

RAB5 is a host dependency factor for the generation of SARS-CoV-2 replication organelles DOI Creative Commons

Yuexuan Chen,

Susanne Klute, Konstantin M. J. Sparrer

et al.

mBio, Journal Year: 2025, Volume and Issue: unknown

Published: April 1, 2025

ABSTRACT Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) remains a threat due to the emergence of variants with increased transmissibility and enhanced escape from immune responses. Like other coronaviruses before, SARS-CoV-2 likely emerged after its transmission bats. The successful propagation in humans might have been facilitated by usurping evolutionarily conserved cellular factors execute crucial steps life cycle, such as generation replication organelles—membrane structures where assemble their replication-transcription complex. In this study, we found that RAB5, which is highly across mammals, critical host dependency factor for genome. Our results also suggest uses RAB5 + membranes build organelles aid COPB1, component COP-I complex, virus protein NSP6 participates process. Hence, targeting represents promising approach interfere RNA synthesis halt propagation. IMPORTANCE sought identify severe organelles: membranous builds order support transcription We uncovered an important organelles, viral target replication.

Language: Английский

Citations

0

Rapid-response RNA-fluorescence in situ hybridization (FISH) assay platform for coronavirus antiviral high-throughput screening DOI Creative Commons
Ryan Chan, Christian Shema Mugisha,

Vorada Chuenchob

et al.

SLAS DISCOVERY, Journal Year: 2024, Volume and Issue: 29(8), P. 100189 - 100189

Published: Nov. 4, 2024

Language: Английский

Citations

1

A coronaviral pore-replicase complex links RNA synthesis and export from double-membrane vesicles DOI Creative Commons

A. Chen,

Ana‐Mihaela Lupan, Rui Tong Quek

et al.

Science Advances, Journal Year: 2024, Volume and Issue: 10(45)

Published: Nov. 8, 2024

Coronavirus-infected cells contain double-membrane vesicles (DMVs) that are key for viral RNA replication and transcription, perforated by hexameric pores connecting the vesicular lumen to cytoplasm. How form traverse two membranes, how DMVs organize synthesis, is unknown. Using structure prediction functional assays, we show nonstructural membrane protein nsp4 pore organizer, spanning double forming most of lining. Nsp4 interacts with nsp3 on cytoplasmic side replicase inside DMV. Newly synthesized mRNAs exit DMV into cytoplasm, passing through a narrow ring conserved residues. Steric constraints imposed predict modified nucleobases block mRNA transit, resulting in broad-spectrum anticoronaviral activity.

Language: Английский

Citations

1

A Coronaviral Pore-Replicase Complex Drives RNA Synthesis in Double Membrane Vesicles DOI Creative Commons

A. Chen,

Ana‐Mihaela Lupan, Rui Tong Quek

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: June 18, 2024

Abstract Coronavirus-infected cells contain double-membrane vesicles (DMVs) that are key for viral RNA replication and transcription, perforated by hexameric pores connecting the vesicular lumen to cytoplasm. How form traverse two membranes, how DMVs organize synthesis, is unknown. Using structure prediction functional assays, we show non-structural membrane protein nsp4 DMV pore organizer, spanning double forming most of lining. Nsp4 interacts with nsp3 on cytoplasmic side replicase inside DMV. Newly synthesized mRNAs exit into cytoplasm, passing through a narrow ring conserved residues. Steric constraints imposed predict modified nucleobases block mRNA transit, broad spectrum anti-coronaviral activity.

Language: Английский

Citations

0