Evidence map›Paper›PMID 34270629›Full record

ArticlePLoS pathogens2021

CryoEM structure of the Nipah virus nucleocapsid assembly.

De-Sheng Ker, Huw T Jenkins, Sandra J Greive, Alfred A Antson

Abstract read
In one paragraph

Article in PLoS pathogens, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

De-Sheng KerYork Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.ORCID 0000-0002-6564-4056
Huw T JenkinsYork Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.ORCID 0000-0002-3302-6966
Sandra J GreiveYork Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.
Alfred A AntsonYork Structural Biology Laboratory, Department of Chemistry, University of York, York, United Kingdom.ORCID 0000-0002-4533-3816

Funding

Wellcome Trust 206377Wellcome Trust 206377/Z/17/Z
6 · The paper itself

Abstract

Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 Å resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the "3-bases-in, 3-bases-out" conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed α-helix, residues 123-139, which may serve as a valuable epitope for surveillance and diagnostics.

Indexed as

Cryoelectron MicroscopyModels, MolecularMolecular ConformationNipah VirusNucleocapsidNucleocapsid ProteinsRNA, ViralNucleocapsid ProteinsRNA, Viral

Identifiers

PMID34270629
PMCPMC8318291

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.