Evidence map›Paper›PMID 24594604›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Structural basis of Flavivirus NS1 assembly and antibody recognition.

Melissa A Edeling, Michael S Diamond, Daved H Fremont

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
12.8field-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

79 citing papers in PubMed, 153 citations in OpenAlex.

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19 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Melissa A EdelingDepartments of Pathology and Immunology, Medicine, Molecular Microbiology, and Biochemistry and Molecular Biophysics, Washington University in St. Louis, St. Louis, MO 63110.
Michael S Diamond
Daved H Fremont
Apath (United States) · USWashington University in St. Louis · US

Funding

Antibody-based Protection against FlavivirsesR01AI073755 · NIAID · WASHINGTON UNIVERSITY · PI DIAMOND, MICHAEL S, FREMONT, DAVED H. · 2007 to 2022
$11.4M
NIAID NIH HHS HHSN272200700058CNIAID NIH HHS HHSN272201200026CNIAID NIH HHS R01 AI073755
6 · The paper itself

Abstract

The Flavivirus nonstructural protein 1 (NS1) is a conserved, membrane-associated and secreted glycoprotein with replication and immune evasion functions. Secreted NS1 is a hexameric, barrel-shaped lipoprotein that can bind back to the plasma membrane of cells. Antibodies targeting cell surface-associated NS1 can be protective in vivo in a manner dependent on Fc effector functions. We describe here the crystal structure of a C-terminal fragment (residues 172-352) of West Nile (WNV) and Dengue virus NS1 proteins at 1.85 and 2.7 Å resolution, respectively. NS1(172-352) assembles as a unique rod-shaped dimer composed of a 16-stranded β-platform flanked on one face by protruding connecting loops. We also determined the 3.0 Å resolution structure of WNV NS1(172-352) with the protective 22NS1 antibody Fab, which engages the loop-face of the rod. The head-to-head NS1(172-352) dimer we observe in crystal lattices is supported by multiangle light and small-angle X-ray scattering studies. We used the available cryo-electron microscopy reconstruction to develop a pseudoatomic model of the NS1 hexamer. The model was constructed with the NS1(172-352) dimeric rod aligned with the long axis of the barrel, and with the loop-face oriented away from the core. Difference densities suggest that the N-terminal region of NS1 forms globular lobes that mediate lateral contacts between dimers in the hexamer. Our model also suggests that the N-terminal lobe forms the surface of the central cavity where lipid binding may occur.

Indexed as

Models, MolecularProtein ConformationAmino Acid SequenceAntibodies, ViralCryoelectron MicroscopyCrystallizationDengue VirusDimerizationGene Expression Regulation, ViralMolecular Sequence DataSequence AlignmentViral Nonstructural ProteinsWest Nile virusAntibodies, Viralnonstructural protein 1, West Nile virusViral Nonstructural Proteinshuman pathogenimmune epitopestructural biologyvirology

Identifiers

PMID24594604
PMCPMC3964132
OpenAlexW2153106062

What OpenQuestion holds

Textmetadata
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.