Abstract
Lma-p18 is an epicuticular surface protein specific to the tergal gland aphrodisiac secretion of Leucophaea maderae adult males. Native Lma-p18 was purified and the complete cDNA sequence was determined by RT-PCR using primers based on Edman degradation fragments. Northern blot and in situ hybridization analyses showed that Lma-p18 is expressed exclusively in the anterior part of male tergal gland, which is exposed only during sexual behavior. Sequence analysis indicated that Lma-p18 belongs to the calycin superfamily and is very similar to Lma-p22, the first known male-specific tergal protein in L. maderae. Lma-p18 and Lma-p22 were proposed to bind different sexually attractive compounds as other calycins.
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