Characterisation of Bombyx mori Odorant-binding Proteins Reveals that a General Odorant-binding Protein Discriminates Between Sex Pheromone Components

Zhou, Jing‐Jiang; Robertson, Giles; He, Xiaoli; Dufour, Samuel; Hooper, Antony M.; Pickett, John A.; Keep, Nicholas H.; Field, L. M.

doi:10.1016/j.jmb.2009.04.015

Cited by 237 publications

(268 citation statements)

References 71 publications

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“…The unparalleled selectivity and sensitivity of bombykol signaling in B. mori, which has long been a paradigm for olfaction in insects (2), is surprising in view of the permissive ways in which BmorPBP binds different lipophilic ligands (24,25) (Fig. 2; hexane as described in Materials and Methods).…”

Section: Discussionmentioning

confidence: 99%

Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein

Damberger

Michel

Ishida

et al. 2013

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

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The Bombyx mori pheromone-binding protein (BmorPBP) is known to adopt two different conformations. These are BmorPBP A , where a regular helix formed by the C-terminal dodecapeptide segment, α7, occupies the ligand-binding cavity, and BmorPBP B , where the binding site is free to accept ligands. NMR spectra of delipidated BmorPBP solutions at the physiological pH of the bulk sensillum lymph near pH 6.5 show only BmorPBP A , and in mixtures, the two species are in slow exchange on the chemical shift frequency scale. This equilibrium has been monitored at variable pH and ligand concentrations, demonstrating that it is an intrinsic property of BmorPBP that is strongly affected by pH variation and ligand binding. This polymorphism tunes BmorPBP for optimal selective pheromone transport: Competition between α7 and lipophilic ligands for its binding cavity enables selective uptake of bombykol at the pore endings in the sensillum wall, whereas compounds with lower binding affinity can only be bound in the bulk sensillum lymph. After transport across the bulk sensillum lymph into the lower pH area near the dendritic membrane surface, bombykol is ejected near the receptor, whereas compounds with lower binding affinity are ejected before reaching the olfactory receptor, rendering them susceptible to degradation by enzymes present in the sensillum lymph.amide proton exchange | conformational equilibrium | insect odorant-binding protein | NMR structure | selective transport of pheromones

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Section: Discussionmentioning

confidence: 99%

Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein

Damberger

Michel

Ishida

et al. 2013

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

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“…The most widely used fluorescent probe is N-phenyl-1-naphthylamine (1-NPN), which has been employed in the binding of Drosophila LUSH (Zhou et al, 2004), the Locusta migratoris LmigOBP1-3 (Jiang et al, 2009;Yu et al, 2009), the social wasp Polistes dominulus OBP1 (Calvello et al, 2003) and Bombyx mori OBPs (Zhou et al, 2009;He et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

Functional characterization and immunolocalization of odorant binding protein 1 in the lucerne plant bug, Adelphocoris lineolatus (GOEZE)

Wang

et al. 2011

Arch Insect Biochem Physiol

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In the insect phylum, the relationships between individuals and their environment are often modulated by chemical communication. Odorant binding proteins (OBPs) are widely and robustly expressed in insect olfactory organs and play a key role in chemosensing and transporting hydrophobic odorants across the sensillum lymph to the olfactory receptor neuron. In this study, a novel OBP gene (AlinOBP1) in the lucerne plant bug, Adelphocoris lineolatus was identified, cloned and expressed. Real-time PCR results indicated that the expression level of AlinOBP1 gene differed in each developmental stage (from first instar to adult) and was predominantly expressed in the antennae of adults. The expression level of AlinOBP1 was 1.91 times higher in male antennae than in female antennae. The binding properties of AlinOBP1 with 114 odorants were measured using a fluorescence probe, N-phenyl-1-naphthylamine (1-NPN), with fluorescence competitive binding. The results revealed that AlinOBP1 exhibits high binding abilities with two major putative pheromone components, ethyl butyrate and trans-2-hexenyl butyrate. In addition, it was observed that six volatiles released from cotton, octanal, nonanal, decanal, 2-ethyl-1-hexanol, b-caryophyllene and b-ionone also bind to AlinOBP1. Immunocytochemistry analysis showed that AlinOBP1 was expressed in the sensillum lymph of sensilla trichodica and sensilla basiconca. Our results demonstrate that AlinOBP1 may function as a carrier in the chemoperception of the lucerne plant bug. C 2011 Wiley Periodicals, Inc.

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“…Pheromone binding protein 1 (PBP1) and general odorant binding protein 2 (GOBP2) were used in the present study. These proteins are present at an extremely high level in antennae compared to others (Zhou, et al, 2009).…”

Section: Obpsmentioning

confidence: 94%

Effective collection of volatile organic compounds in water using rimming flow with odorant-binding proteins

Kida

Tsukada

Tagawa

et al. 2015

Mechanical Engineering Journal

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Water solution of volatile organic compounds (VOCs) in air, especially explosive materials, is required to detect VOCs by biosensors efficiently. We developed a collecting device like olfactory mechanism of animals: thin film of water including odorant binding proteins (OBPs), which play a major role in transport of hydrophobic odor molecules to olfactory receptors. Thin liquid film was generated using rimming flow on the inner surface of a rotating glass cylinder. Two kinds of OBPs derived from Bombyx mori (Pheromone Binding Protein 1: PBP1, General Odorant Binding Protein 2: GOBP2) were used as additive in pure water. Eugenol was used to simulate an explosive substance for collection. The sample gas including dilute eugenol was collected by the rimming flow device. The concentration of eugenol in solution was measured by gas chromatography. The experimental results showed that the efficiency for the collection of eugenol increased with the revolution rate of the cylinder. Increase in the efficiency was mainly attributed to the spread of the liquid in the cylinder. Furthermore, as the revolution rate was increased, the mole fraction of eugenol near the inside wall was higher than at the axis of rotation by centrifugal force. This might enhance the dissolution of eugenol in water. The collection efficiency further increased by the adding of both proteins and PBP1 exhibited higher affinity for eugenol.

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Characterisation of Bombyx mori Odorant-binding Proteins Reveals that a General Odorant-binding Protein Discriminates Between Sex Pheromone Components

Cited by 237 publications

References 71 publications

Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein

Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein

Functional characterization and immunolocalization of odorant binding protein 1 in the lucerne plant bug, Adelphocoris lineolatus (GOEZE)

Effective collection of volatile organic compounds in water using rimming flow with odorant-binding proteins

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