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- Title
Ligand binding to six recombinant pheromone-binding proteins of Antheraea polyphemus and Antheraea pernyi.
- Authors
Maida, R.; Ziegelberger, G.; Kaissling, K.-E.
- Abstract
Binding properties of six heterologously expressed pheromone-binding proteins (PBPs) identified in the silkmoths Antheraea polyphemus and Antheraea pernyi were studied using tritium-labelled pheromone components, (E,Z)-6,11-hexadecadienyl acetate (3H-Ac1) and (E,Z)-6,11-hexadecadienal (3H-Ald), common to both species. In addition, a known ligand of PBP and inhibitor of pheromone receptor cells, the tritium-labelled esterase inhibitor decyl-thio-1,1,1-trifluoropropanone (3H-DTFP), was tested. The binding of ligands was measured after native gel electrophoresis and cutting gel slices. In both species, PBP1 and PBP3 showed binding of 3H-Ac1. In competition experiments with 3H-Ac1 and the third unlabelled pheromone component, (E,Z)-4,9-tetradecadienyl acetate (Ac2), the PBP1 showed preferential binding of Ac1, whereas PBP3 preferentially bound Ac2. The PBP2 of both species bound 3H-Ald only. All of the six PBPs strongly bound 3H-DTFP. Among unlabelled pheromone derivatives, alcohols were revealed to be the best competitors for 3H-Ac1 and 3H-Ald bound to PBPs. No pH influence was found for 3H-Ac1 binding to, or its release from, the PBP3 of A. polyphemus and A. pernyi between pH 4.0 and pH 7.5. The data indicate binding preference of each of the three PBP-subtypes (1–3) for a specific pheromone component and support the idea that PBPs contribute to odour discrimination, although to a smaller extent than receptor activation.
- Subjects
CARRIER proteins; LIGANDS (Biochemistry); PHEROMONES; ANTHERAEA; POLYPHEMUS moth; CHINESE oak silkworm
- Publication
Journal of Comparative Physiology B: Biochemical, Systemic & Environmental Physiology, 2003, Vol 173, Issue 7, p565
- ISSN
0174-1578
- Publication type
Article
- DOI
10.1007/s00360-003-0366-4