Candidate odorant receptors from the malaria vector mosquito Anopheles gambiae and evidence of down-regulation in response to blood feeding
- 27 November 2001
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 98 (25) , 14693-14697
- https://doi.org/10.1073/pnas.261432998
Abstract
Olfaction plays a major role in host preference and blood feeding, integral behaviors for disease transmission by the malaria vector mosquito Anopheles gambiae sensu stricto (henceforth A. gambiae). We have identified four genes encoding candidate odorant receptors from A. gambiae that are selectively expressed in olfactory organs, contain approximately seven transmembrane domains, and show significant similarity to several putative odorant receptors in Drosophila melanogaster. Furthermore, one of the putative A. gambiae odorant receptors exhibits female-specific antennal expression and is down-regulated 12 h after blood feeding, a period during which substantial reduction in olfactory responses to human odorants has been observed. Taken together, these data suggest these genes encode a family of odorant receptors in A. gambiae, whose further study may aid in the design of novel antimalarial programs.Keywords
This publication has 32 references indexed in Scilit:
- A Novel Family of Divergent Seven-Transmembrane ProteinsNeuron, 1999
- ODOR-MEDIATED BEHAVIOR OF AFROTROPICAL MALARIA MOSQUITOESAnnual Review of Entomology, 1999
- Quartet Puzzling: A Quartet Maximum-Likelihood Method for Reconstructing Tree TopologiesMolecular Biology and Evolution, 1996
- Divergent seven transmembrane receptors are candidate chemosensory receptors in C. elegansCell, 1995
- Evolutionary conservation of both the hydrophilic and hydrophobic nature of transmembrane residuesJournal of Theoretical Biology, 1995
- Malaria: Current and Future Prospects for ControlAnnual Review of Entomology, 1995
- A Segment Corresponding to Amino Acids Val170-Arg182 of Bovine Arrestin is Capable of Binding to Phosphorylated RhodopsinEuropean Journal of Biochemistry, 1994
- Basic Local Alignment Search ToolJournal of Molecular Biology, 1990
- Basic local alignment search toolJournal of Molecular Biology, 1990
- A simple method for displaying the hydropathic character of a proteinJournal of Molecular Biology, 1982