Evidence map›Paper›PMID 27102935›Full record

ArticleScientific reports2016

Crystal Structures and Binding Dynamics of Odorant-Binding Protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri.

Tom Northey, Herbert Venthur, Filomena De Biasio, Francois-Xavier Chauviac, Ambrose Cole, Karlos Antonio Lisboa Ribeiro, Gerarda Grossi, Patrizia Falabella, Linda M Field, Nicholas H Keep and 1 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 75 citations in OpenAlex.

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  10. Chemosensory protein 4 is required forFrontiers in physiology · 2022
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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 4 institutions in 3 countries.

Tom NortheyCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London WC1E 7HX, UK.
Herbert VenthurDepartment of Biological Chemistry and Crop Protection, Rothamsted Research, Harpenden, AL5 2JQ, UK.
Filomena De BiasioDepartment of Biological Chemistry and Crop Protection, Rothamsted Research, Harpenden, AL5 2JQ, UK.
Francois-Xavier ChauviacCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London WC1E 7HX, UK.
Ambrose ColeCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London WC1E 7HX, UK.
Karlos Antonio Lisboa RibeiroDepartment of Biological Chemistry and Crop Protection, Rothamsted Research, Harpenden, AL5 2JQ, UK.
Gerarda GrossiDipartimento di Scienze, Università della Basilicata, via dell'Ateneo Lucano 10, 85100 Potenza, Italy.
Patrizia FalabellaDipartimento di Scienze, Università della Basilicata, via dell'Ateneo Lucano 10, 85100 Potenza, Italy.
Linda M FieldDepartment of Biological Chemistry and Crop Protection, Rothamsted Research, Harpenden, AL5 2JQ, UK.
Nicholas H KeepCrystallography, Institute for Structural and Molecular Biology, Department of Biological Sciences, Birkbeck, University of London, London WC1E 7HX, UK.
Jing-Jiang ZhouDepartment of Biological Chemistry and Crop Protection, Rothamsted Research, Harpenden, AL5 2JQ, UK.
Birkbeck, University of London · GBRothamsted Research · GBUniversity of Basilicata · ITUniversidad de La Frontera · CL

Funding

Biotechnology and Biological Sciences Research Council BB/D005892/1
6 · The paper itself

Abstract

Aphids use chemical cues to locate hosts and find mates. The vetch aphid Megoura viciae feeds exclusively on the Fabaceae, whereas the currant-lettuce aphid Nasonovia ribisnigri alternates hosts between the Grossulariaceae and Asteraceae. Both species use alarm pheromones to warn of dangers. For N. ribisnigri this pheromone is a single component (E)-β-farnesene but M. viciae uses a mixture of (E)-β-farnesene, (-)-α-pinene, β-pinene, and limonene. Odorant-binding proteins (OBP) are believed to capture and transport such semiochemicals to their receptors. Here, we report the first aphid OBP crystal structures and examine their molecular interactions with the alarm pheromone components. Our study reveals some unique structural features: 1) the lack of an internal ligand binding site; 2) a striking groove in the surface of the proteins as a putative binding site; 3) the N-terminus rather than the C-terminus occupies the site closing off the conventional OBP pocket. The results from fluorescent binding assays, molecular docking and dynamics demonstrate that OBP3 from M. viciae can bind to all four alarm pheromone components and the differential ligand binding between these very similar OBP3s from the two aphid species is determined mainly by the direct π-π interactions between ligands and the aromatic residues of OBP3s in the binding pocket.

Indexed as

AphidsAnimalsFluorometryInsect ProteinsKineticsModels, MolecularMolecular Docking SimulationPheromonesProtein BindingProtein ConformationReceptors, OdorantInsect Proteinsodorant-binding proteinPheromonesReceptors, Odorant

Identifiers

PMID27102935
PMCPMC4840437
OpenAlexW2340549330

What OpenQuestion holds

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LicenceCC BY
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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.