Ultrastructure Characteristics and Sexual Dimorphism of Antennal Sensilla in Tirathaba rufivena (Lepidoptera: Pyralidae).

Tirathaba rufivena Walker, a major insect pest of Areca catechu L., has severely threatened areca nut cultivation in Hainan, China. To improve our understanding of the communication mechanism in host plant seeking and mate-finding for T. rufivena, we described and further characterized the external morphology and internal sensilla structures using scanning electron microscopy and transmission electron microscopy in this study. The antennal morphology was similar between males and females, and there was no significant difference in length between the two sexes. In total, nine sensilla types were identified: sensilla trichodea (Str), sensilla chaetica (Sch), sensilla basiconica (Sba), sensilla auricillica (Sau), sensilla coeloconica (Sco), sensilla styloconica (Sst), Böhm sensilla (Bs), uniporous peg sensilla (Ups) and sensilla squamiformia (Ssq). Sexual dimorphism mainly occurs in variation in the length of Sba, Sch, Sco1 and Bs, and the abundance of Sba, Sau1 and Sau2. The Sba had larger size and numbers on female antennae than that on males, suggesting that these sensilla might have important roles in locating host plants. Both Sau1 and Sau2 were significantly more abundant in females and were probably associated with the detection of mates and host plant for oviposition. These data were important for ongoing studies on host plant seeking and mate-finding behavior in T. rufivena and provided a theoretical foundation to further studies of semiochemical control for this pest.

Binding Properties of Odorant-Binding Protein 4 of Tirathaba rufivena to Areca catechu Volatiles.

Odorant-binding proteins (OBPs) play a key role in the olfactory system and are essential for mating and oviposition host selection. Tirathaba rufivena, a serious lepidopterous insect pest of the palm area in recent years, has threatened cultivations of Areca catechu in Hainan. Female-biased odorant-binding protein 4 of T. rufivena (TrufOBP4) expression was hypothesized to participate in the process of oviposition host recognition and localization. In this study, we cloned and analyzed the cDNA sequence of TrufOBP4. The predicted mature protein TrufOBP4 is a small, soluble, secretory protein and belongs to a classic OBP subfamily. Fluorescence binding assay results showed that TrufOBP4 had high binding abilities with the host plant volatiles, octyl methoxycinnamate, dibutyl phthalate, myristic acid and palmitic acid. These four components tend to dock in the same binding pocket based on the molecular docking result. The interactions and contributions of key amino acid residues were also characterized. This research provides evidence that TrufOBP4 might participate in the chemoreception of volatile compounds from inflorescences of A. catechu and can contribute to the integrated management of T. rufivena.