Pheromone-PBP complex

Mechanism of pheromone binding and release 15.3.1 The pheromone-PBP complex... 

Recently, a putative olfactory receptor from Drosophila, Or43a (Clyne et al., 1999 Vosshall et al., 1999), has been expressed in Xenopus laevis oocytes (Wetzel et al., 2001). The receptor expressed in a heterologous cell system was activated by four odorants, i.e. cyclohexanone, cyclohexanol, benzaldehyde, and benzyl alcohol (Wetzel et al., 2001). These experiments not only provided direct evidence for the function of the Or gene, but also demonstrated that the olfactory receptor can be stimulated without an odorant-binding protein. It was demonstrated earlier that PBP was not necessary to obtain pheromone-dependent responses in cultured olfactory receptor neurons of Manduca sexta (Stengl et al., 1992). The possibility that OBPs have been produced in vitro and were present in cultured ORNs could not be excluded. The same argument can not be raised for the heterologous expression of the Drosophila olfactory receptor. While the evidence that Xenopus oocytes responded to odorants in the absence of OBPs does not support the OBP-odorant complex model, it also demonstrated that OBPs are essential for the kinetics of the olfactory system (see below). 

An antenna remains in a plume 1 s and an antenna is not an isolated system, as is required to reach equilibrium. The kinetic properties of the PBP-ligand complexes may be more important to the function of PBPs as potential filters than the equilibrium dissociation constants. Thus, ligands with very fast association rate constants and very slow dissociation rate constants are more likely to be bound at the pore surfaces and to traverse the sensillar lymph unharmed by the powerful pheromone-degrading enzymes in the lymph (see below). Thus, in order to understand the function of PBPs, it is essential to obtain more data on binding kinetics. 

Sandler B. H., Nikonova L., Leal W. S. and Clardy J. (2000) Sexual attraction in the silkworm moth structure of the PBP-pheromone-binding-protein-bombykol complex. Chemistry Biol. 7, 143-151. 

---