A molecular pore spans the double membrane of the coronavirus replication organelle
View ORCID ProfileGeorg Wolff1, View ORCID ProfileRonald W. A. L. Limpens1, Jessika C. Zevenhoven-Dobbe2, View ORCID ProfileUlrike Laugks3, View ORCID ProfileShawn Zheng4, View ORCID ProfileAnja W. M. de Jong1, View ORCID ProfileRoman I. Koning1, View ORCID ProfileDavid A. Agard5, View ORCID ProfileKay Grünewald3,6, View ORCID ProfileAbraham J. Koster1, View ORCID ProfileEric J. Snijder2, View ORCID ProfileMontserrat Bárcena1,*
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Science 06 Aug 2020:
eabd3629
DOI: 10.1126/science.abd3629
Abstract
Coronavirus genome replication is associated with virus-induced cytosolic double-membrane vesicles, which may provide a tailored micro-environment for viral RNA synthesis in the infected cell. However, it is unclear how newly synthesized genomes and mRNAs can travel from these sealed replication compartments to the cytosol to ensure their translation and the assembly of progeny virions. Here, we used cellular electron cryo-microscopy to visualize a molecular pore complex that spans both membranes of the double-membrane vesicle and would allow export of RNA to the cytosol. A hexameric assembly of a large viral transmembrane protein was found to form the core of the crown-shaped complex. This coronavirus-specific structure likely plays a critical role in coronavirus replication and thus constitutes a potential drug target.
