Molecular characterization of a male-specific glycosyl hydrolase, Lma-p72, secreted on to the abdominal surface of the Madeira cockroach Leucophaea maderae (Blaberidae, Oxyhaloinae).

The epicuticular surface protein Lma-p72 is specific to the abdominal secretions of Leucophaea maderae (Madeira cockroach) adult males. Natural Lma-p72 was purified and the complete cDNA sequence determined by reverse-transcription PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p72 was expressed in the tergal and sternal glands. Sequence alignment indicates that Lma-p72 is closely related to the family 1 glycosyl hydrolases (EC 3.2.1). Native Lma-p72 was proved to be active in the abdominal secretions and exhibit a beta-galactosidase-like activity. However, weak specificity with respect to the C-4 configuration of the substrate was observed. Two main hypotheses were proposed concerning the function of this enzyme: Lma-p72 could hydrolyse oligosaccharides from the male abdominal secretions, making them more phagostimulatory for the female during the precopulatory behaviour. The protein could also cleave a pheromone-sugar conjugate to release the pheromonal compounds on to the cuticular surface. Such a sugar conjugate could be a transport form. Data from the first in vivo inhibition tests indicate that a glycosidase could be directly involved in the production process of some pheromonal compounds in L. maderae males.