Immunocytochemical localization of pheromone-binding protein in moth antennae

Steinbrecht, Rudolf Alexander; Ozaki, Mamiko; Ziegelberger, Gunde

doi:10.1007/bf00328015

Cited by 172 publications

(111 citation statements)

References 57 publications

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“…Both OS-E and OS-F are present in the sensillum lymph of sensory hairs housing olfactory receptor neurons as well as in the underlying auxiliary cells. Most likely, OS-E and OS-F are soluble proteins synthesized by the sensillar auxiliary cells, which then secrete them into the sensillar lymph surrounding the olfactory receptor neurons, as also is believed to be the case for the moth OBPs (Steinbrecht et al, 1992(Steinbrecht et al, , 1995Laue et al, 1994).…”

Section: Discussionmentioning

confidence: 94%

“…In moths, different functional classes of sensilla express different classes of OBPs. The pheromone-binding proteins are associated with pheromonesensitive sensilla-primarily the specialized sensilla trichodea of the males (Steinbrecht et al, 1992)-whereas another group of OBPs, termed general odorant-binding proteins, is associated with sensilla that respond to general odorants-primarily the sensilla basiconica present in males and females (Laue et al, 1994;Steinbrecht et al, 1995). This distinction between PBP or GOBP expression seems to reflect a difference in sensillar function rather than simply a property of the morphological type.…”

Section: Discussionmentioning

confidence: 99%

“…PBPs and GOBPs are present at high concentrations in the sensillar lymph surrounding the dendrites of receptor cells tuned to pheromones or general odorants, respectively (Laue et al, 1994;Steinbrecht et al, 1992Steinbrecht et al, , 1995.…”

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confidence: 99%

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Coexpression of Two Odorant-Binding Protein Homologs inDrosophila: Implications for Olfactory Coding

1997

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Odorant-binding proteins (OBPs) are small soluble proteins present in the aqueous medium surrounding olfactory receptor neurons. Their function in olfaction is still unknown: they have been proposed to facilitate the transit of hydrophobic molecules to olfactory receptors, to deactivate the odorant stimulus, and/or to play a role in chemosensory coding. In this study we examine the genomic organization and expression patterns of two olfactory-specific genes (OS-E and OS-F ) of Drosophila melanogaster, the products of which are members of a protein family in Drosophila sharing sequence similarity with moth OBPs. We show that the OS-E and OS-F transcription units are located Ͻ1 kb apart. They are oriented in the same direction and display a similar intron-exon organization. Expression of both OS-E and OS-F proteins is restricted spatially to the ventrolateral region of the Drosophila antenna. Within this region both OS-E and OS-F proteins are expressed within two different types of sensory hairs: in most, if not all, sensilla trichodea and in ϳ40% of the interspersed small sensilla basiconica. We consistently observe that OS-E and OS-F are coexpressed, indicating that an individual sensillum can contain more than one odorant-binding protein. The functional significance of the observed expression pattern and its implications for olfactory coding are discussed.

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Section: Discussionmentioning

confidence: 94%

Section: Discussionmentioning

confidence: 99%

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Coexpression of Two Odorant-Binding Protein Homologs inDrosophila: Implications for Olfactory Coding

1997

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“…Immunocytochemical localisation of OBPs has been determined in Lepidoptera where pheromone-sensitive sensilla trichodea express PBPs (Steinbrecht et al 1992), whereas sensilla basiconica mainly express GOBPs (Laue et al 1994). No co-localisation of PBPs and GOBPs in the same sensillum has been observed (Steinbrecht et al 1995).…”

Section: Odour Coding and Neural Connectionsmentioning

confidence: 99%

Olfaction in vector-host interactions

Takken¹,

Knols²

2010

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“…There is no direct evidence that they have 8-barrel structures, but von Ebner's gland protein and OBP were reported to have eight putative 8-sheets and are presumed to belong to the same family as the retinol-binding protein and 8-lactoglobulin, etc [7]. The PBPs have five and six putative 8-sheets, respectively [24], and it has been noted that the insect-derived members are likely to be classified into a different family than the vertebrate-derived members [9, 2.51. The insect-derived members might not have the characteristic 8-barrel structure but a different type of conformation, in which, besides the 8-sheets, disulfide bonds would be important to support or maintain the tertiary structure.…”

Section: Discussionmentioning

confidence: 99%

A Putative Lipophilic Stimulant Carrier Protein Commonly Found in the Taste and Olfactory Systems. A Unique Member of the Pheromone-binding Protein Superfamily

Ozaki¹,

Morisaki²,

Idei³

et al. 1995

Eur J Biochem

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In chemosensory systems, a variety of lipophilic ligand-binding proteins have been found in saliva or nasal mucus. Lipophilic stimulants reach the receptor membrane, carried by these proteins. An acidic 14-kDa protein purified in the blowfly, Phormia regina, belongs to the insect pheromone-binding protein superfamily, but unlike other lipohilic ligand-binding proteins in insect or vertebrate chemosensory systems, it was distributed in both taste and olfactory organs. A similar protein was also isolated in Drosophila melanogaster: Considering their distributions, cDNA sequences and structural features, we concluded that these proteins belong to a unique subfamily whose members have convergently evolved for a common function required for both senses of taste and olfaction. By an electrophysiological experiment using antiserum, we also suggested that these proteins carry fragrant components of natural foods in taste systems as well as in olfactory systems.

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Immunocytochemical localization of pheromone-binding protein in moth antennae

Cited by 172 publications

References 57 publications

Coexpression of Two Odorant-Binding Protein Homologs inDrosophila: Implications for Olfactory Coding

Coexpression of Two Odorant-Binding Protein Homologs inDrosophila: Implications for Olfactory Coding

Olfaction in vector-host interactions

A Putative Lipophilic Stimulant Carrier Protein Commonly Found in the Taste and Olfactory Systems. A Unique Member of the Pheromone-binding Protein Superfamily

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