Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories

Jingru Fang, Guillaume Castillon, Sebastien Phan, Sara McArdle, Chitra Hariharan, Aiyana Adams, Mark H. Ellisman, Ashok A. Deniz and Erica Ollmann Saphire ()
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Jingru Fang: La Jolla Institute for Immunology
Guillaume Castillon: University of California San Diego, School of Medicine
Sebastien Phan: University of California San Diego, School of Medicine
Sara McArdle: La Jolla Institute for Immunology
Chitra Hariharan: La Jolla Institute for Immunology
Aiyana Adams: La Jolla Institute for Immunology
Mark H. Ellisman: University of California San Diego, School of Medicine
Ashok A. Deniz: Scripps Research
Erica Ollmann Saphire: La Jolla Institute for Immunology

Nature Communications, 2023, vol. 14, issue 1, 1-16

Abstract: Abstract Ebola virus (EBOV) infection induces the formation of membrane-less, cytoplasmic compartments termed viral factories, in which multiple viral proteins gather and coordinate viral transcription, replication, and assembly. Key to viral factory function is the recruitment of EBOV polymerase, a multifunctional machine that mediates transcription and replication of the viral RNA genome. We show that intracellularly reconstituted EBOV viral factories are biomolecular condensates, with composition-dependent internal exchange dynamics that likely facilitates viral replication. Within the viral factory, we found the EBOV polymerase clusters into foci. The distance between these foci increases when viral replication is enabled. In addition to the typical droplet-like viral factories, we report the formation of network-like viral factories during EBOV infection. Unlike droplet-like viral factories, network-like factories are inactive for EBOV nucleocapsid assembly. This unique view of EBOV propagation suggests a form-to-function relationship that describes how physical properties and internal structures of biomolecular condensates influence viral biogenesis.

Date: 2023
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DOI: 10.1038/s41467-023-39821-7

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