Purification and molecular cloning of chemosensory proteins fromBombyx mori

Picimbon, Jean-François; Dietrich, Karen; Angeli, Sergio; Scaloni, Andrea; Krieger, Jürgen; Breer, Heinz; Pelosi, Paolo

doi:10.1002/1520-6327(200007)44:3<120::aid-arch3>3.0.co;2-h

Cited by 77 publications

(60 citation statements)

References 37 publications

(49 reference statements)

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“…The general name of chemosensory proteins (CSPs) was proposed for this class of polypeptides to include roles in both olfaction and taste [54]. CSPs have since been isolated and cloned in several insect species, belonging to different orders, such as Lepidoptera [55][56][57][58][59][60], Hymenoptera [37,[61][62][63][64][65], Blattoidea [50,66,67], Orthoptera [54,[68][69][70] and Hemiptera [71]. CSPs are smaller than OBPs, with 100-120 residues and bear no sequence similarity to OBPs.…”

Section: Chemosensory Proteinsmentioning

confidence: 69%

“…In Diptera, the number of OBPs is much higher than the number of CSPs (51 OBPs vs. 4 CSPs in D. melanogaster, and 57 OBPs vs. 7 CSPs in A. gambiae). In Lepidoptera, 10 different CSPs have been cloned from tissue samples of Mamestra brassicae [59], and the same number of genes is present in the genome of B. mori [22,57]. Five CSP ESTs have been found in M. sexta [58], but only one CSP has been reported in Cactoblastis cactorum [55].…”

Section: Chemosensory Proteinsmentioning

confidence: 99%

“…This, however, seems not to be a problem because both OBPs and CSPs do not carry post-translational modifications apart from the establishment of disulphide bridges [37,53,54,57,69]. Moreover, it has been experimentally demonstrated that such bridges form spontaneously in the same pattern observed in the natural proteins [37].…”

Section: Ligand Bindingmentioning

confidence: 99%

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Soluble proteins in insect chemical communication

Pelosi

Zhou

Ban

et al. 2006

Cell. Mol. Life Sci.

762

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Our understanding of the biochemical mechanisms that mediate chemoreception in insects has been greatly improved after the discovery of olfactory and taste receptor proteins. However, the presence of soluble polypeptides in high concentration around the dendrites of sensory neurons still poses unanswered questions. More than 2 decades after their discovery and despite the wealth of structural information available, the physiological function of odorant-binding proteins is not well understood. More recently, members of a second family of soluble polypeptides, the chemosensory proteins, were also discovered in the lymph of chemosensilla. Here we review the structural properties of both classes of soluble proteins, their affinity to small ligands, and their expression in the different parts of the insect body and subcellular localisation. Finally, we discuss current ideas and models of the role of such proteins in insect chemoreception.

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Section: Chemosensory Proteinsmentioning

confidence: 69%

Section: Chemosensory Proteinsmentioning

confidence: 99%

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Soluble proteins in insect chemical communication

Pelosi

Zhou

Ban

et al. 2006

Cell. Mol. Life Sci.

762

728

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“…Gustatory sensilla chaetica expressing CSP, on the other hand, are found on most parts of the body including wings, legs and ovipositor. In most insect species, OBPs are specifically expressed in the antennae and therefore have been associated with olfaction, whereas CSPs are expressed also in other body parts [7,33]. However, this is not always the case, as in some Hymenoptera, such as the argentine ant Linepithema humile and in the paper wasp Polistes dominulus, the situation is reversed: CSP is antenna-specific, while OBP is expressed in different parts of the body [34][35][36]; immunocytochemical data for these species are so far not available.…”

Section: Discussionmentioning

confidence: 99%

Expression and immunolocalisation of odorant-binding and chemosensory proteins in locusts

Jin

Brandazza

Navarrini

et al. 2005

CMLS, Cell. Mol. Life Sci.

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We have identified, cloned and expressed a new chemosensory protein (CSP) in the desert locust Schistocerca gregaria belonging to a third sub-class of these polypeptides. Polyclonal antibodies stained a band of 14 kDa, as expected, in the extracts of antennae and palps of the adults, but not in the 4th and 5th instars. In the related species Locusta migratoria, instead, the same antibodies cross-reacted only with a band of apparent molecular mass of 35 kDa in the extract of 1st-5th instars, but not in the adults. The recombinant protein binds the fluorescent probe N-phenyl-1-naphthylamine, but none of the compounds so far reported as pheromones for S. gregaria. The expression of the odorant-binding protein (OBP) and of CSPs of sub-classes I and II was also monitored in antennae, tarsi, palpi, wings and other organs of solitary and gregarious locusts in their nymphal and adult stages. OBP was found to be antenna specific, where it is expressed at least from the 3rd instar in both solitary and gregarious locusts. CSPs, instead, appear to be more ubiquitous, with different expression patterns, according to the sub-class. Immunocytochemistry experiments revealed that OBP is present in the sensillum lymph of sensilla trichodea and basiconica, while CSP-I and CSP-III were found in the outer sensillum lymph of sensilla chaetica and in the sub-cuticular space between epidermis and cuticle of the antenna. Sensilla chaetica on other parts of the body showed the same expression of CSP-I as those on the antenna.

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“…C hemosensory proteins (CSPs) have been identified in antennae from Drosophila melanogaster and in antennae, proboscis, tarsi, and labrum from several insects (1)(2)(3)(4)(5)(6)(7). Several CSPs from antenna or proboscis have also been isolated in the moth Mamestra brassicae (3).…”

mentioning

confidence: 99%

Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding

Campanacci

Lartigue

Hållberg

et al. 2003

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

146

152

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Chemosensory proteins (CSPs) have been proposed to transport hydrophobic chemicals from air to olfactory or taste receptors. They have been isolated from several sensory organs of a wide range of insect species. The x-ray structure of CSPMbraA6, a 112-aa antennal protein from the moth Mamestra brassicae (Mbra), was shown to exhibit a novel type of ␣-helical fold. We have performed a structural and binding study of CSPMbraA6 to get some insights into its possible molecular function. Tryptophan fluorescence quenching demonstrates the ability of CSPMbraA6 to bind several types of semio-chemicals or surrogate ligands with M Kd. Its crystal structure in complex with one of these compounds, 12-bromo-dodecanol, reveals extensive conformational changes on binding, resulting in the formation of a large cavity filled by three ligand molecules. Furthermore, binding cooperativity was demonstrated for some ligands, suggesting a stepwise binding. The peculiar rearrangement of CSPMbraA6 conformation and the cooperativity phenomenon might trigger the recognition of chemicals by receptors and induce subsequent signal transduction.

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Purification and molecular cloning of chemosensory proteins fromBombyx mori

Cited by 77 publications

References 37 publications

Soluble proteins in insect chemical communication

Soluble proteins in insect chemical communication

Expression and immunolocalisation of odorant-binding and chemosensory proteins in locusts

Moth chemosensory protein exhibits drastic conformational changes and cooperativity on ligand binding

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