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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.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-020-18243-9

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Role:
Author
ORCID:
0000-0003-4854-590X
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Role:
Author
ORCID:
0000-0003-0220-8844
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Role:
Author
ORCID:
0000-0002-4480-5439


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
11
Article number:
4445
Publication date:
2020-09-07
Acceptance date:
2020-08-08
DOI:
EISSN:
2041-1723
Pmid:
32895380


Language:
English
Keywords:
Pubs id:
1131254
Local pid:
pubs:1131254
Deposit date:
2021-07-14
ARK identifier:

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