Assembly intermediates of orthoreovirus captured in the cell

Geoff Sutton, Dapeng Sun, Xiaofeng Fu, Abhay Kotecha, Corey W. Hecksel, Daniel K. Clare, Peijun Zhang (), David I. Stuart () and Mark Boyce ()
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Geoff Sutton: University of Oxford
Dapeng Sun: University of Pittsburgh
Xiaofeng Fu: University of Pittsburgh
Abhay Kotecha: University of Oxford
Corey W. Hecksel: Harwell Science and Innovation Campus
Daniel K. Clare: Harwell Science and Innovation Campus
Peijun Zhang: University of Oxford
David I. Stuart: University of Oxford
Mark Boyce: University of Oxford

Nature Communications, 2020, vol. 11, issue 1, 1-7

Abstract: Abstract Traditionally, molecular assembly pathways for viruses are inferred from high resolution structures of purified stable intermediates, low resolution images of cell sections and genetic approaches. Here, we directly visualise an unsuspected ‘single shelled’ intermediate for a mammalian orthoreovirus in cryo-preserved infected cells, by cryo-electron tomography of cellular lamellae. Particle classification and averaging yields structures to 5.6 Å resolution, sufficient to identify secondary structural elements and produce an atomic model of the intermediate, comprising 120 copies each of protein λ1 and σ2. This λ1 shell is ‘collapsed’ compared to the mature virions, with molecules pushed inwards at the icosahedral fivefolds by ~100 Å, reminiscent of the first assembly intermediate of certain prokaryotic dsRNA viruses. This supports the supposition that these viruses share a common ancestor, and suggests mechanisms for the assembly of viruses of the Reoviridae. Such methodology holds promise for dissecting the replication cycle of many viruses.

Date: 2020
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DOI: 10.1038/s41467-020-18243-9

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