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.
Cornette
Richard
R
C.N.R.S., U.M.R. 5548, 'Développement - Communication Chimique', Université de Bourgogne, 6 boulevard Gabriel, 21000 Dijon, France.
Farine
Jean-Pierre
JP
Abed-Viellard
Dehbia
D
Quennedey
Brigitte
B
Brossut
Rémy
R
D000818:Animals; D001692:Biological Transport; D015152:Blotting, Northern; D003058:Cockroaches / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary / Q000235:genetics; D004848:Epithelium / Q000502:physiology; D005088:Exocrine Glands / Q000201:enzymology; D005260:Female; D005942:Gluconates / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000235:genetics* / Q000378:metabolism; D006838:Hydrocarbons / Q000494:pharmacology; D017403:In Situ Hybridization; D019476:Insect Proteins / Q000235:genetics* / Q000378:metabolism; D007783:Lactones; D007814:Larva; D008297:Male; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000378:metabolism; D010675:Pheromones / Q000737:chemistry / Q000378:metabolism; D016133:Polymerase Chain Reaction; D011994:Recombinant Proteins / Q000737:chemistry; D001616:beta-Galactosidase / Q000378:metabolism
D018076:DNA, Complementary; D005942:Gluconates; D006838:Hydrocarbons; D019476:Insect Proteins; D007783:Lactones; D009844:Oligosaccharides; D010675:Pheromones; D011994:Recombinant Proteins; D006026:Glycoside Hydrolases; D001616:beta-Galactosidase; C010730:beta-glucono-1,5-lactone