BIROn - Birkbeck Institutional Research Online

    Crystal structures and binding dynamics of Odorant-Binding Protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri

    Northey, Thomas and Venthur, H. and De Biasio, F. and Chauviac, Francois-Xavier and Cole, Ambrose and Lisboa Ribeiro Junior, K.A. and Grossi, G. and Falabella, P. and Field, L.M. and Keep, Nicholas H. and Zhou, J.J. (2016) Crystal structures and binding dynamics of Odorant-Binding Protein 3 from two aphid species Megoura viciae and Nasonovia ribisnigri. Scientific Reports 6 , p. 24739. ISSN 2045-2322.

    [img] Text
    ApisOBP3Structure_MergedFile_62313_2_merged_1457717469.pdf - Author's Accepted Manuscript
    Restricted to Repository staff only
    Available under License Creative Commons Attribution.

    Download (7MB)
    [img]
    Preview
    Text
    14853A.pdf - Published Version of Record
    Available under License Creative Commons Attribution.

    Download (1MB) | Preview

    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 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.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): odorant-binding protein, aphid, (E)-ß-farnesene, crystal structure, molecular docking, repellent, binding pocket
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Nicholas Keep
    Date Deposited: 22 Apr 2016 12:34
    Last Modified: 20 Sep 2019 23:53
    URI: http://eprints.bbk.ac.uk/id/eprint/14853

    Statistics

    Downloads
    Activity Overview
    102Downloads
    120Hits

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item