Molecular Basis of Pheromone Detection in Insects

Vogt, Richard G.

doi:10.1016/b0-44-451924-6/00047-8

Cited by 139 publications

(189 citation statements)

References 420 publications

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“…AB734104). This secreted protein had six cysteine residues that are observed in those of the Classic OBP family (8,20). However, Blastp search, ClustalW alignment, and phylogenetic tree analyses indicated that this protein had 92% amino acid sequence identity with a NPC2-like protein from C. floridanus (GenBank accession no.…”

Section: Resultsmentioning

confidence: 99%

“…The sensillum cavity is completely segregated from the hemocoel by the membranes of tormogen, thecogen, trichogen cells, and receptor dendrite, and it is filled with aqueous sensillum lymph (7). Odorant-binding proteins (OBPs) and chemosensory proteins (CSPs) that accumulate in the sensillum cavity play essential roles in transferring semiochemicals to the Or/odorant receptor coreceptor (Orco) complex, a ligand-gated ion channel on the receptor membrane (8)(9)(10)(11)(12). OBPs and CSPs are composed of α-helices that are knitted with disulfide bridges.…”

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confidence: 99%

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Niemann–Pick type C2 protein mediating chemical communication in the worker ant

Ishida

Tsuchiya

Fujii

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

104

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Ants are eusocial insects that are found in most regions of the world. Within its caste, worker ants are responsible for various tasks that are required for colony maintenance. In their chemical communication, α-helical carrier proteins, odorant-binding proteins, and chemosensory proteins, which accumulate in the sensillum lymph in the antennae, play essential roles in transferring hydrophobic semiochemicals to chemosensory receptors. It has been hypothesized that semiochemicals are recognized by α-helical carrier proteins. The number of these proteins, however, is not sufficient to interact with a large number of semiochemicals estimated from chemosensory receptor genes. Here we shed light on this conundrum by identifying a Niemann–Pick type C2 (NPC2) protein from the antenna of the worker Japanese carpenter ant, Camponotus japonicus (CjapNPC2). CjapNPC2 accumulated in the sensillum cavity in the basiconic sensillum. The ligand-binding pocket of CjapNPC2 was composed of a flexible β-structure that allowed it to bind to a wide range of potential semiochemicals. Some of the semiochemicals elicited electrophysiolgical responses in the worker antenna. In vertebrates, NPC2 acts as an essential carrier protein for cholesterol from late endosomes and lysosomes to other cellular organelles. However, the ants have evolved an NPC2 with a malleable ligand-binding pocket as a moderately selective carrier protein in the sensillum cavity of the basiconic sensillum. CjapNPC2 might be able to deliver various hydrophobic semiochemicals to chemosensory receptor neurons and plays crucial roles in chemical communication required to perform the worker ant tasks.

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Niemann–Pick type C2 protein mediating chemical communication in the worker ant

Ishida

Tsuchiya

Fujii

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

104

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“…Such dendrites are housed in specialized structures of the cuticle, the olfactory sensillum (Steinbrecht, 1992), filled with lymph, whose major components are small acidic proteins. These proteins belong to two major families of OBPs (odorant-binding proteins) with molecular weights around 15-16 kDa and smaller CSPs (chemosensory proteins) of about 11-13 kDa (for recent reviews, see : Pelosi et al, 2006;Picimbon, 2003;Vogt, 2003Vogt, , 2005Leal, 2005;Tegoni et al, 2004). The concentration of such proteins in the sensillum lymph has been estimated to reach values as high as 5-10 mM (Klein, 1987).…”

Section: Introductionmentioning

confidence: 98%

New isoforms of odorant‐binding proteins and potential semiochemicals of locusts

Cui

Jiang

et al. 2007

Arch Insect Biochem Physiol

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To obtain more information on the elements of chemical communication in the migratory locust (Locusta migratoria) (Orthoptera: Acrididae), we have searched for additional odorant-binding proteins (OBPs) and for volatiles in the feces that could represent potential semiochemicals for this species. A two-dimensional electrophoretic (2DE) analysis of an antennal extract showed only three closely positioned spots that were recognized by the antiserum against locust OBP. Three genes were also identified using PCR and 5'RACE-PCR approaches, encoding isoforms differing from each other for a single amino acid substitution. The gas-chromatographic-electroantennogram (GC-EAD) headspace analysis of a feces sample revealed the presence of several compounds that elicited dose-dependent electrophysiological responses in the antennae of both sexes. Most of these compounds are different from those identified in the feces of the desert locust (Schistocerca gregaria) and reported to be behaviorally active. Ligand-binding experiments performed with such volatiles and recombinant OBP did not show affinity, thus indicating that the binding pocket of OBP requires larger molecules than those so far identified.

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“…Considering a suggestion in the elephant (Lazar et al, 2002), Vogt (2005) proposed a conjecture that some odor-OBP complexes may sequester ligand as a deactivator. Together with the high concentration of OBP, which is up to 10 mM in vivo (Klein, 1987), the protection of ligand from enzyme degradation and the ability of transformation from different conformations, it is worth considering that OBPs can be a candidate for ligand deactivator.…”

Section: Pheromone Deactivation and Protection From Enzymatic Degradamentioning

confidence: 99%

Review An overview of odorant-binding protein functions in insect peripheral olfactory reception

Fan¹,

Francis²,

Liu³

et al. 2011

Genet. Mol. Res.

171

129

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ABSTRACT. Insect olfactory perception involves many aspects of insect life, and can directly or indirectly evoke either individual or group behaviors. Insect olfactory receptors and odorant-binding proteins (OBPs) are considered to be crucial to insect-specific and -sensitive olfaction. Although the mechanisms of interaction between OBPs or OBP/ligand complex with olfactory receptors are still not well understood, it has been shown that many OBPs contribute to insect olfactory perception at various levels. Some of these are numerous and divergent members in OBP family; expression in the olfactory organ at high concentration; a variety of combinational patterns between different OBPs and ligands, but exclusive affinity for one OBP to specific binding ligands; complicated interactions between OBP/ligand complex and transmembrane proteins (olfactory receptors or sensory neuron membrane proteins). First, we review OBPs' ligand-binding property based on OBP structural research and ligandbinding test; then, we review current progress around the points cited above OBP functions in insect peripheral olfactory reception to show the role of such proteins in insect olfactory signal transmission; finally, we discuss applications based on insect OBP research.

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Molecular Basis of Pheromone Detection in Insects

Cited by 139 publications

References 420 publications

Niemann–Pick type C2 protein mediating chemical communication in the worker ant

Niemann–Pick type C2 protein mediating chemical communication in the worker ant

New isoforms of odorant‐binding proteins and potential semiochemicals of locusts

Review An overview of odorant-binding protein functions in insect peripheral olfactory reception

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