For the first time, a termite sex pheromone secreted by tergal glands has been isolated and identified. In the mandibulate nasute termite Cornitermes bequaerti, pairing of swarming imagoes is mediated by a sex pheromone secreted by females from their tergal glands. These well developed sexual glands located in front of tergites 8, 9, 10 are essentially composed of class 1 and 2 cells, but also of some glandular units of class 3 cells. The major volatile compound of tergal secretion was isolated by solid phase microextraction (SPME) and identified by GC-MS as (3Z, 6Z, 8E)-dodecatrien-1-ol. Sex attraction bioassays with synthetic (3Z, 6Z, 8E)-dodecatrien-1-ol showed that this alcohol was the main component of the sex pheromone in C. bequaerti. The cellular origin and the key role of (3Z, 6Z, 8E)-dodecatrien-1-ol in the biology of termites are discussed.

In Coleoptera, the elytra (forewings), with a very hard and thick cuticle, protect the membranous and delicate hindwings against mechanical stress. We have isolated and characterized a cDNA encoding a major cuticle protein in Tenebrio molitor, named ACP‐20. The deduced amino acid sequence is roughly tripartite, with two terminal glycine‐rich domains and a central region showing pronounced similarities with some other hard cuticle proteins. Northern blot and in situ hybridization analyses reveal that ACP‐20 gene expression is developmentally regulated since transcript accumulation occurs only in epidermal regions synthesizing hard cuticle and is restricted to the period of preecdysial adult cuticle deposition. Moreover, application of a juvenile hormone analogue prevents the appearance of the transcript, indicating that juvenile hormone, a key molecule involved in the control of insect metamorphosis, negatively regulates the expression of the ACP‐20 gene.

The complete sequence of a cDNA clone, isolated from epidermal mRNA of Tenebrio molitor using a monoclonal antibody raised against an adult-specific cuticular antigen only present in the hard cuticle, was obtained after primer extension at the 5' end. From this cDNA sequence, the deduced protein encompasses 199 amino acids (including a signal peptide) with a total molecular weight of 20.7 kDa. The protein exhibits a bipartite structure: glycine-rich region located in its NH2-terminal part and a carboxy-terminal domain sharing homologies with other cuticular proteins of Orthoptera, Diptera and Lepidoptera. In-situ hybridization analysis shows that the corresponding mRNA is present only in epidermal cells secreting the adult fibrous cuticle destined to become heavily sclerotized. In supernumerary pupae obtained after the application of the juvenile hormone analogue (JHA) to newly ecdysed pupae, the mRNA was undetectable, indicating that JHA can prevent the switch to the adult programme. However, in pupal-adult intermediates, obtained when JHA is applied later, the mRNA is detected.

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