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Salivary gland transcripts of the kissing bug, Panstrongylus chinai, a vector of Chagas disease
- Kato, Hirotomo, Jochim, Ryan C., Gomez, Eduardo A., Tsunekawa, Shunsuke, Valenzuela, Jesus G., Hashiguchi, Yoshihisa
- Acta tropica 2017
- Chagas disease, Panstrongylus, Rhodnius prolixus, Triatoma, anticoagulants, antigens, apyrase, blood meal, cDNA libraries, clones, complementary DNA, hematophagous arthropods, inositols, medicinal properties, platelet aggregation, protein secretion, proteinase inhibitors, proteins, saliva, salivary glands, serine proteinases
- The saliva of blood sucking arthropods contains potent pharmacologically active components to counteract the host hemostatic and inflammatory systems when they take a blood meal. In the present study, dominant salivary gland transcripts of Panstrongylus chinai, a vector of Chagas disease, were analyzed by sequencing randomly selected clones of the salivary gland cDNA library. This analysis showed that 56.5% of the isolated transcripts coded for putative secreted proteins, of which 73.7% coded for proteins belonging to the lipocalin family. The most abundant transcript of lipocalin family proteins was a homologue of pallidipin 2, an inhibitor of collagen-induced platelet aggregation of Triatoma pallidipennis. In addition, homologues of triafestin, an inhibitor of the kallikrein-kinin system of T. infestans, were identified as the dominant transcript. Other salivary transcripts encoding lipocalin family proteins had homology to triplatin (an inhibitor of platelet aggregation) and others with unknown function. Other than lipocalin family proteins, homologues of a Kazal-type serine protease inhibitor (putative anticoagulant), a hemolysin-like protein (unknown function), inositol polyphosphate 5-related protein (a regulator of membrane phosphoinositide), antigen 5-related protein (unknown function) and apyrase (platelet aggregation inhibitor) were identified.