Evidence map›Paper›PMID 26849049›Full record

ArticlePLoS pathogens2016

Acidic pH-Induced Conformations and LAMP1 Binding of the Lassa Virus Glycoprotein Spike.

Sai Li, Zhaoyang Sun, Rhys Pryce, Marie-Laure Parsy, Sarah K Fehling, Katrin Schlie, C Alistair Siebert, Wolfgang Garten, Thomas A Bowden, Thomas Strecker and 1 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
10.7field-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

96 citing papers in PubMed, 131 citations in OpenAlex.

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  14. Architectural organization andJournal of virology · 2024
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  18. Strategies of rational and structure-driven vaccine design for Arenaviruses.Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases · 2024
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  20. Article

36 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

11 authors at 3 institutions in 2 countries.

Sai LiDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Zhaoyang SunDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Rhys PryceDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Marie-Laure ParsyDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Sarah K FehlingInstitute of Virology, Philipps Universität Marburg, Marburg, Germany.
Katrin SchlieInstitute of Virology, Philipps Universität Marburg, Marburg, Germany.
C Alistair SiebertDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Wolfgang GartenInstitute of Virology, Philipps Universität Marburg, Marburg, Germany.
Thomas A BowdenDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Thomas StreckerInstitute of Virology, Philipps Universität Marburg, Marburg, Germany.
Juha T HuiskonenDivision of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford, United Kingdom.
Philipps University of Marburg · DEUniversity of Oxford · GBCentre for Human Genetics · GB

Funding

Medical Research Council MR/J007897/1Medical Research Council MR/L009528/1Wellcome TrustWellcome Trust 060208/Z/00/ZWellcome Trust 093305/Z/10/Z
6 · The paper itself

Abstract

Lassa virus is an enveloped, bi-segmented RNA virus and the most prevalent and fatal of all Old World arenaviruses. Virus entry into the host cell is mediated by a tripartite surface spike complex, which is composed of two viral glycoprotein subunits, GP1 and GP2, and the stable signal peptide. Of these, GP1 binds to cellular receptors and GP2 catalyzes fusion between the viral envelope and the host cell membrane during endocytosis. The molecular structure of the spike and conformational rearrangements induced by low pH, prior to fusion, remain poorly understood. Here, we analyzed the three-dimensional ultrastructure of Lassa virus using electron cryotomography. Sub-tomogram averaging yielded a structure of the glycoprotein spike at 14-Å resolution. The spikes are trimeric, cover the virion envelope, and connect to the underlying matrix. Structural changes to the spike, following acidification, support a viral entry mechanism dependent on binding to the lysosome-resident receptor LAMP1 and further dissociation of the membrane-distal GP1 subunits.

Indexed as

Protein Sorting SignalsAnimalsChlorocebus aethiopsGlycoproteinsHydrogen-Ion ConcentrationLassa virusLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsModels, MolecularMolecular ConformationMultiprotein ComplexesProtein BindingProtein Structure, TertiaryVero CellsViral Envelope ProteinsVirionGlycoproteinsLAMP1 protein, humanLysosomal-Associated Membrane Protein 1Lysosomal Membrane ProteinsMultiprotein ComplexesProtein Sorting SignalsViral Envelope Proteins

Identifiers

PMID26849049
PMCPMC4743923
OpenAlexW2257256261

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.