Evidence map›Paper›PMID 33784403›Full record

ArticleNucleic acids research2021

Crystal structures of influenza nucleoprotein complexed with nucleic acid provide insights into the mechanism of RNA interaction.

Yun-Sang Tang, Shutong Xu, Yu-Wai Chen, Jia-Huai Wang, Pang-Chui Shaw

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 10% of its field
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

30 citing papers in PubMed, 42 citations in OpenAlex.

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  17. Negative and ambisense RNA virus ribonucleocapsids: more than protective armor.Microbiology and molecular biology reviews : MMBR · 2023
    Review
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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

5 authors at 3 institutions in 3 countries.

Yun-Sang TangCentre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong SAR, China.
Shutong XuDepartment of Medical Oncology and Department of Cancer Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
Yu-Wai ChenDepartment of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hong Kong SAR, China.
Jia-Huai WangDepartment of Medical Oncology and Department of Cancer Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115, USA.
Pang-Chui ShawCentre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong SAR, China.
Chinese University of Hong Kong · HKHarvard University · USHong Kong Polytechnic University · HK

Funding

Structures of Alpha 4 Integrins, Ligands and AntagonistsP01HL103526 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI SPRINGER, TIMOTHY A · 2011 to 2015
$11.1M
NHLBI NIH HHS P01 HL103526
6 · The paper itself

Abstract

The nucleoprotein (NP) of influenza virus is the core component of the ribonucleoprotein (RNP) and performs multiple structural and functional roles. Structures of the influenza A, B and D NP molecules have been solved previously, but structural information on how NP interacts with RNA remains elusive. Here we present the crystal structure of an obligate monomer of H5N1 NP in complex with RNA nucleotides to 2.3 Å, and a C-terminal truncation of this mutant, also in complex with RNA nucleotides, to 3 Å. In both structures, three nucleotides were identified near two positive grooves of NP suggested to be important for RNA binding. Structural evidence supports that conformational changes of flexible loops and the C-terminal tail both play important roles in the binding of RNA. Based on the structure, we propose a mechanism by which NP captures RNA by flexible loops and transfers it onto the positive binding grooves. Binding of RNA by NP is a crucial step for template re-encapsidation during transcription and replication and cRNP formation. Our structures thus provide insights into the molecular virology of the influenza virus.

Indexed as

Influenza A Virus, H5N1 SubtypeModels, MolecularNucleoproteinsProtein BindingProtein ConformationRNA, ViralNucleoproteinsRNA, Viral

Identifiers

PMID33784403
PMCPMC8053115
OpenAlexW3148225421

What OpenQuestion holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.