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Mosquitoes & moths OBP database (mOBPdb)
Welcome to the database for odorant binding proteins (OBPs) from mosquitoes and moths.
The molecular basis of the odorant perception of mosquitoes and moths is encoded by a series of proteins. One of the members considered very important in this process are the odorant binding proteins (OBPs) which are believed to aid in the transport of odorants and pheromones to the odorant receptors (ORs) and have emerged as novel targets for repellants.
We are here reporting a manually curated database of OBPs for mosquitoes and moths.
Among the mosquito OBPs, we report 69 OBPs in Anopheles gambiae, 111 OBPs in the Aedes aegypti and 109 OBPs in the Culex quinquefasciatus genomes [1]. We also report OBPs from other species of the Anopheles genus: A. albimanus, A. arabiensis, A. atroparvus, A. christyi, A. coluzzii, A. culicifacies A, A. darlingi, A. dirus, A. epiroticus, A. funestus, A. maculatus, A. melas, A. merus, A. minimus, A. quadriannulatus, A. sinensis, A. stephensi.
We are currently adding OBPs from three moths species: Bombyx mori, Bombyx mandarina, Manduca sexta.
There are 3 families of odorant binding proteins in mosquitoes and moths:
- the Classic OBPs
- the PlusC OBPs
- the Two-domains also know as duplex (OBPs formerly known as the Atypical OBPs)
The hallmark of OBPs are their conserved 6 cysteines that forms 3 disulphide bridges.However the number of cysteines and the disulphide connectivity patterns of the OBPs vary among the different subfamilies. Click here for a graphical illustration. A subgroup in the Classic OBPs called the MinusC OBPs and a subgroup in the two domain OBP subfamily called the matype2 do not have all the six conserved cysteines in their OBP domains. Atypical odorant binding proteins are in fact two-domain or duplex OBPs, where each domain is distantly related to the Classic OBPs.
We are providing in this database
- full genomic data (list of OBP genes, chromosomal or supercontig localization, sequence alignment data, phylogenetic data and orthologues).
- functional characterization of all Classic OBPs from mosquitoes model species Anopheles gambiae, Aedes aegypti and Culex quinquifasciatus screened against a large library of 126 odorants known to be repellents and attractants using molecular docking technique together with corresponding free energies of binding (FEB), Ki values (i.e Kd), size-independant ligand binding efficiencies values and PDB files of corresponding protein-odorant complexes.
Results for subsequent ligand screening is not yet available for Classic OBPs from other mosquito species and for all PlusC and Two-domains (duplex formerly know as atypical) OBPs. We are currently working to make them available soon.
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Contact details
Bernard Offmann (bernard.offmann ‘@’ univ-nantes.fr)
Developping team
Head: Bernard Offmann (Nantes Université, France), Sowdhamini Ramanathan (NCBS – TIFR, India)
Current students: Mikhael Djemoussi, Maelle Belaud, Gabriel Rollin
Former students: Malini Manoharan, Matthieu Ng Fuk Cheong, Aurore Vaïtinadapoullé, Etienne Frumence, Olivier Cadet, Nicolas Belouin, Charlotte Berthelier, Amandine Lecerf Defer, Bavikha Mam, Surbhi Dhingra, Marine Averty, Nicolas Antunes, Damien Rat, Julien Louet
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