Evidence map›Paper›PMID 36347841›Full record

ArticleNature communications2022

CryoEM structures of the multimeric secreted NS1, a major factor for dengue hemorrhagic fever.

Bo Shu, Justin S G Ooi, Aaron W K Tan, Thiam-Seng Ng, Wanwisa Dejnirattisai, Juthathip Mongkolsapaya, Guntur Fibriansah, Jian Shi, Victor A Kostyuchenko, Gavin R Screaton and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
12.6field-weighted citation impact, top 1% 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

35 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  8. Dengue and severe dengue.Clinical microbiology reviews · 2025
    Review
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  19. Functional Roles and Host Interactions ofPathogens (Basel, Switzerland) · 2025
    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

11 authors at 2 institutions in 2 countries.

Bo ShuProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore.
Justin S G OoiProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore.ORCID 0000-0003-4899-8255
Aaron W K TanProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore.ORCID 0000-0002-4046-7380
Thiam-Seng NgProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore.ORCID 0000-0002-1668-8976
Wanwisa DejnirattisaiMedical Sciences Division, University of Oxford, Oxford, OX3 9D, UK.
Juthathip MongkolsapayaMedical Sciences Division, University of Oxford, Oxford, OX3 9D, UK.ORCID 0000-0003-3416-9480
Guntur FibriansahProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore.ORCID 0000-0002-9990-3335
Jian ShiCentre for Bioimaging Sciences, Department of Biological Sciences, National University of Singapore, Singapore, 117557, Singapore.
Victor A KostyuchenkoProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore.
Gavin R ScreatonMedical Sciences Division, University of Oxford, Oxford, OX3 9D, UK.ORCID 0000-0002-3549-4309
Shee-Mei LokProgramme in Emerging Infectious Diseases, Duke-National University of Singapore Medical School, Singapore, 169857, Singapore. sheemei.lok@duke-nus.edu.sg.ORCID 0000-0003-4631-8041
National University of Singapore · SGUniversity of Oxford · GB

Funding

Wellcome Trust 203224/Z/16/Z
6 · The paper itself

Abstract

Dengue virus infection can cause dengue hemorrhagic fever (DHF). Dengue NS1 is multifunctional. The intracellular dimeric NS1 (iNS1) forms part of the viral replication complex. Previous studies suggest the extracellular secreted NS1 (sNS1), which is a major factor contributing to DHF, exists as hexamers. The structure of the iNS1 is well-characterised but not that of sNS1. Here we show by cryoEM that the recombinant sNS1 exists in multiple oligomeric states: the tetrameric (stable and loose conformation) and hexameric structures. Stability of the stable and loose tetramers is determined by the conformation of their N-terminal domain - elongated β-sheet or β-roll. Binding of an anti-NS1 Fab breaks the loose tetrameric and hexameric sNS1 into dimers, whereas the stable tetramer remains largely unbound. Our results show detailed quaternary organization of different oligomeric states of sNS1 and will contribute towards the design of dengue therapeutics.

Indexed as

DengueDengue VirusNoonan SyndromeSevere DengueHumansViral Nonstructural ProteinsViral Nonstructural Proteins

Identifiers

PMID36347841
PMCPMC9643530
OpenAlexW4308736831

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.