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Assembly intermediates of orthoreovirus captured in the cell.

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.

journal_name

Nat Commun

journal_title

Nature communications

authors

Sutton G,Sun D,Fu X,Kotecha A,Hecksel CW,Clare DK,Zhang P,Stuart DI,Boyce M

doi

10.1038/s41467-020-18243-9

subject

Has Abstract

pub_date

2020-09-07 00:00:00

pages

4445

issue

1

issn

2041-1723

pii

10.1038/s41467-020-18243-9

journal_volume

11

pub_type

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