Pheromone binding proteins of the moth Mamestra brassicae: Specificity of ligand binding

Maı̈bèche-Coisné, Martine; Sobrio, Franck; Delaunay, Thierry; Lettere, Martine; Dubroca, Jacqueline; Jacquin‐Joly, Emmanuelle; Meillour, Patricia Nagnan‐Le

doi:10.1016/s0965-1748(96)00088-4

Cited by 75 publications

(49 citation statements)

References 34 publications

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“…These results are in contrast with previous studies suggesting that pheromone discrimination might occur not only at a receptor level, but also in the first molecular step, i.e. binding of pheromones to PBPs (8,(21)(22)(23)(24)(37)(38)(39). Concerning MbraPBP1, migration on native gels and autoradiography indicated that the antennal protein was able to bind the tritiated major pheromonal compound, Z11-C16-Ac (38).…”

Section: Discussioncontrasting

confidence: 99%

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Revisiting the Specificity of Mamestra brassicaeand Antheraea polyphemus Pheromone-binding Proteins with a Fluorescence Binding Assay

Campanacci

Krieger

Bette

et al. 2001

Journal of Biological Chemistry

197

185

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Pheromone-binding proteins (PBPs), located in the sensillum lymph of pheromone-responsive antennal hairs, are thought to transport the hydrophobic pheromones to the chemosensory membranes of olfactory neurons. It is currently unclear what role PBPs may play in the recognition and discrimination of speciesspecific pheromones. We have investigated the binding properties and specificity of PBPs from Mamestra brassicae (MbraPBP1), Antheraea polyphemus (ApolPBP1), Bombyx mori (BmorPBP), and a hexa-mutant of MbraPBP1 (Mbra1-M6), mutated at residues of the internal cavity to mimic that of BmorPBP, using the fluorescence probe 1-aminoanthracene (AMA). AMA binds to MbraPBP1 and ApolPBP1, however, no binding was observed with either BmorPBP or Mbra1-M6. The latter result indicates that relatively limited modifications to the PBP cavity actually interfere with AMA binding, suggesting that AMA binds in the internal cavity. Several pheromones are able to displace AMA from the MbraPBP1-and ApolPBP1-binding sites, without, however, any evidence of specificity for their physiologically relevant pheromones. Moreover, some fatty acids are also able to compete with AMA binding. These findings bring into doubt the currently held belief that all PBPs are specifically tuned to distinct pheromonal compounds.

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Section: Discussioncontrasting

confidence: 99%

“…binding of pheromones to PBPs (8,(21)(22)(23)(24)(37)(38)(39). Concerning MbraPBP1, migration on native gels and autoradiography indicated that the antennal protein was able to bind the tritiated major pheromonal compound, Z11-C16-Ac (38). However, since this was the only compound tested, the result should be taken with caution.…”

Section: Discussionmentioning

confidence: 96%

Revisiting the Specificity of Mamestra brassicaeand Antheraea polyphemus Pheromone-binding Proteins with a Fluorescence Binding Assay

Campanacci

Krieger

Bette

et al. 2001

Journal of Biological Chemistry

197

185

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“…This is the first binding data obtained for an insect olfactory-binding protein other than lepidoptera PBPs. A large number of such PBPs have been shown to bind components of the sex pheromone (Vogt and Riddiford, 1981;Vogt et al, 1989;Feixas et al, 1995;Pretswich et al, 1995;Maïbèche-Coisne et al, 1997). Pheromone binding properties of gOBPs are not so well documented.…”

Section: Pheromone Binding Properties Of Recombinant Asp1mentioning

confidence: 99%

Cloning and Expression of a Queen Pheromone-Binding Protein in the Honeybee: an Olfactory-Specific, Developmentally Regulated Protein

et al. 1999

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Odorant-binding proteins (OBPs) are small abundant extracellular proteins thought to participate in perireceptor events of odor-pheromone detection by carrying, deactivating, and/or selecting odor stimuli. The honeybee queen pheromone is known to play a crucial role in colony organization, in addition to drone sex attraction. We identified, for the first time in a social insect, a binding protein called antennal-specific protein 1 (ASP1), which binds at least one of the major queen pheromone components. ASP1 was characterized by cDNA cloning, expression in Pichia pastoris, and pheromone binding. In situ hybridization showed that it is specifically expressed in the auxiliary cell layer of the antennal olfactory sensilla. The ASP1 sequence revealed it as a divergent member of the insect OBP family. The recombinant protein presented the exact characteristics of the native protein, as shown by mass spectrometry, and N-terminal sequencing and exclusion-diffusion chromatography showed that recombinant ASP1 is dimeric. ASP1 interacts with queen pheromone major components, opposite to another putative honeybee OBP, called ASP2. ASP1 biosynthetic accumulation, followed by nondenaturing electrophoresis during development, starts at day 1 before emergence, in concomitance with the functional maturation of olfactory neurons. The isobar ASP1b isoform appears simultaneously to ASP1a in workers, but only at ϳ2 weeks after emergence in drones. Comparison of in vivo and heterologous expressions suggests that the difference between ASP1 isoforms might be because of dimerization, which might play a physiological role in relation with mate attraction.

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“…For example, five OBPs have been described in the moth Antheraea pernyi Raming et al 1990;Krieger et al 1991Krieger et al , 1997. Several studies have shown that the different OBPs found within a single insect species display distinct odorant-binding specificities Prestwich et al 1995;Maïbeche-Coisne et al 1997;Plettner et al 2000). Furthermore, Drosophila that lack the "LUSH" OBP show specific deficits in response to the odorants ethanol or benzaldehyde (Kim et al 1998;Wang et al 2001).…”

mentioning

confidence: 99%

Genome-Wide Analysis of the Odorant-Binding Protein Gene Family in Drosophila melanogaster

Hekmat-Scafe¹,

Scafe²,

McKinney³

et al. 2002

Genome Res.

411

404

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Olfaction is of considerable importance to many insects in behaviors critical for survival and reproduction, including location of food sources, selection of mates, recognition of colony con-specifics, and determination of oviposition sites. An ubiquitous, but poorly understood, component of the insect's olfactory system is a group of odorant-binding proteins (OBPs) that are present at high concentrations in the aqueous lymph surrounding the dendrites of olfactory receptor neurons. OBPs are believed to shuttle odorants from the environment to the underlying odorant receptors, for which they could potentially serve as odorant presenters. Here we show that the Drosophila genome carries 51 potential OBP genes, a number comparable to that of its odorant-receptor genes. We find that the majority (73%) of these OBP-like genes occur in clusters of as many as nine genes, in contrast to what has been observed for the Drosophila odorant-receptor genes. Two of the presumptive OBP gene clusters each carries an odorant-receptor gene. We also report an intriguing subfamily of 12 putative OBPs that share a unique C-terminal structure with three conserved cysteines and a conserved proline. Members of this subfamily have not previously been described for any insect. We have performed phylogenetic analyses of the OBP-related proteins in Drosophila as well as other insects, and we discuss the duplication and divergence of the genes for this large family.

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Pheromone binding proteins of the moth Mamestra brassicae: Specificity of ligand binding

Cited by 75 publications

References 34 publications

Revisiting the Specificity of Mamestra brassicaeand Antheraea polyphemus Pheromone-binding Proteins with a Fluorescence Binding Assay

Revisiting the Specificity of Mamestra brassicaeand Antheraea polyphemus Pheromone-binding Proteins with a Fluorescence Binding Assay

Cloning and Expression of a Queen Pheromone-Binding Protein in the Honeybee: an Olfactory-Specific, Developmentally Regulated Protein

Genome-Wide Analysis of the Odorant-Binding Protein Gene Family in Drosophila melanogaster

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