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« Previous AbstractCharacterization of Volatile Organic Compounds in Five Celery (Apium graveolens L.) Cultivars with Different Petiole Colors by HS-SPME-GC-MS    Next AbstractA lysine at the C-terminus of an odorant-binding protein is involved in binding aldehyde pheromone components in two Helicoverpa species »

PLoS One


Title:Expression in antennae and reproductive organs suggests a dual role of an odorant-binding protein in two sibling Helicoverpa species
Author(s):Sun YL; Huang LQ; Pelosi P; Wang CZ;
Address:"State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, Beijing, China"
Journal Title:PLoS One
Year:2012
Volume:20120123
Issue:1
Page Number:e30040 -
DOI: 10.1371/journal.pone.0030040
ISSN/ISBN:1932-6203 (Electronic) 1932-6203 (Linking)
Abstract:"Odorant-binding proteins (OBPs) mediate both perception and release of semiochemicals in insects. These proteins are the ideal targets for understanding the olfactory code of insects as well as for interfering with their communication system in order to control pest species. The two sibling Lepidopteran species Helicoverpa armigera and H. assulta are two major agricultural pests. As part of our aim to characterize the OBP repertoire of these two species, here we focus our attention on a member of this family, OBP10, particularly interesting for its expression pattern. The protein is specifically expressed in the antennae of both sexes, being absent from other sensory organs. However, it is highly abundant in seminal fluid, is transferred to females during mating and is eventually found on the surface of fertilised eggs. Among the several different volatile compounds present in reproductive organs, OBP10 binds 1-dodecene, a compound reported as an insect repellent. These results have been verified in both H. armigera and H. assulta with no apparent differences between the two species. The recombinant OBP10 binds, besides 1-dodecene, some linear alcohols and several aromatic compounds. The structural similarity of OBP10 with OBP1 of the mosquito Culex quinquefasciatus, a protein reported to bind an oviposition pheromone, and its affinity with 1-dodecene suggest that OBP10 could be a carrier for oviposition deterrents, favouring spreading of the eggs in these species where cannibalism is active among larvae"
Keywords:"Amino Acid Sequence Animals Arthropod Antennae/*metabolism Culicidae/*genetics/growth & development/metabolism Female Gene Expression/physiology *Genetic Speciation Genitalia, Female/*metabolism Male Molecular Sequence Data Phylogeny Receptors, Odorant/ge;"
Notes:"MedlineSun, Ya-Lan Huang, Ling-Qiao Pelosi, Paolo Wang, Chen-Zhu eng Research Support, Non-U.S. Gov't 2012/02/01 PLoS One. 2012; 7(1):e30040. doi: 10.1371/journal.pone.0030040. Epub 2012 Jan 23"

 
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