Dataset Information

Melt With This Kiss: Paralyzing and Liquefying Venom of The Assassin Bug Pristhesancus plagipennis (Hemiptera: Reduviidae).

ABSTRACT: Assassin bugs (Hemiptera: Heteroptera: Reduviidae) are venomous insects, most of which prey on invertebrates. Assassin bug venom has features in common with venoms from other animals, such as paralyzing and lethal activity when injected, and a molecular composition that includes disulfide-rich peptide neurotoxins. Uniquely, this venom also has strong liquefying activity that has been hypothesized to facilitate feeding through the narrow channel of the proboscis-a structure inherited from sap- and phloem-feeding phytophagous hemipterans and adapted during the evolution of Heteroptera into a fang and feeding structure. However, further understanding of the function of assassin bug venom is impeded by the lack of proteomic studies detailing its molecular composition.By using a combined transcriptomic/proteomic approach, we show that the venom proteome of the harpactorine assassin bug Pristhesancus plagipennis includes a complex suite of >100 proteins comprising disulfide-rich peptides, CUB domain proteins, cystatins, putative cytolytic toxins, triabin-like protein, odorant-binding protein, S1 proteases, catabolic enzymes, putative nutrient-binding proteins, plus eight families of proteins without homology to characterized proteins. S1 proteases, CUB domain proteins, putative cytolytic toxins, and other novel proteins in the 10-16-kDa mass range, were the most abundant venom components. Thus, in addition to putative neurotoxins, assassin bug venom includes a high proportion of enzymatic and cytolytic venom components likely to be well suited to tissue liquefaction. Our results also provide insight into the trophic switch to blood-feeding by the kissing bugs (Reduviidae: Triatominae). Although some protein families such as triabins occur in the venoms of both predaceous and blood-feeding reduviids, the composition of venoms produced by these two groups is revealed to differ markedly. These results provide insights into the venom evolution in the insect suborder Heteroptera.

SUBMITTER: Walker AA

PROVIDER: S-EPMC5383778 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature

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Publications

Melt With This Kiss: Paralyzing and Liquefying Venom of The Assassin Bug <i>Pristhesancus plagipennis</i> (Hemiptera: Reduviidae).

Walker Andrew A AA Madio Bruno B Jin Jiayi J Undheim Eivind A B EA Fry Bryan G BG King Glenn F GF

Molecular & cellular proteomics : MCP 20170127 4

Assassin bugs (Hemiptera: Heteroptera: Reduviidae) are venomous insects, most of which prey on invertebrates. Assassin bug venom has features in common with venoms from other animals, such as paralyzing and lethal activity when injected, and a molecular composition that includes disulfide-rich peptide neurotoxins. Uniquely, this venom also has strong liquefying activity that has been hypothesized to facilitate feeding through the narrow channel of the proboscis-a structure inherited from sap- an ...[more]

PMID: 28130397

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Project description:The New World assassin bug genus Zelus Fabricius, 1803 (Insecta: Hemiptera: Heteroptera: Reduviidae: Harpactorinae: Harpactorini) is revised based on more than 10,000 specimens. Seventy-one species are recognized and twenty-four described as new: Zelus aithaleos sp. n., Zelus amblycephalus sp. n., Zelus antiguensis sp. n., Zelus auralanus sp. n., Zelus bahiaensis sp. n., Zelus banksi sp. n., Zelus casii sp. n., Zelus championi sp. n., Zelus cordazulus sp. n., Zelus fuliginatus sp. n., Zelus gilboventris sp. n., Zelus gracilipes sp. n., Zelus grandoculus sp. n., Zelus kartaboides sp. n., Zelus lewisi sp. n., Zelus panamensis sp. n., Zelus paracephalus sp. n., Zelus rosulentus sp. n., Zelus russulumus sp. n., Zelus spatulosus sp. n., Zelus truxali sp. n., Zelus umbraculoides sp. n., Zelus umbraculus sp. n., and Zelus xouthos sp. n. Five species, Zelus araneiformis Haviland, 1931, Zelus gradarius Bergroth, 1905, Zelus modestus (Stål, 1862), Zelus subfasciatus Stål, 1860 and Zelus vittaticeps Stål, 1866, are removed from Zelus and placed incertae sedis within Harpactorini. Nine new synonyms are recognized (senior synonym in parentheses): Zelus atripes Champion, 1898 syn. nov. (=Zelus conjungens [Stål, 1860]), Zelus dispar Fabricius, 1803 syn. nov. (=Zelus pedestris Fabricius, 1803), Zelus formosus Haviland, 1931 syn. nov. (=Zelus laticornis Herrich-Schaeffer, 1853), Zelus obscuridorsis (Stål, 1860) syn. nov. (=Zelus pedestris), Zelus pallidinervus Haviland, 1931 syn. nov. (=Zelus kartabensis Haviland, 1931), Zelus personatus Berg, 1879 syn. nov. (=Zelus versicolor Herrich-Schaeffer, 1848), Zelus trimaculatus Champion, 1898 syn. nov. (=Zelus means Fabricius, 1803), Zelus trimaculicollis (Stål, 1855) syn. nov. (=Zelus means), and Zelus tristis Haviland, 1931 syn. nov. (=Zelus laticornis). Zelus conjungens (Stål, 1860) stat. rev. Is resurrected from junior synonymy with zealous armillatus (Lepeletier & Seville, 1825). Zelus ambulans Stål, 1862 stat. rev. and Zelus cognatus (Costa, 1862) stat. rev. are resurrected from synonymy with Zelus exsanguis Stål, 1862. Iquitozelus Bérenger syn. nov. is synonymized with Zelus and its only species transferred to Zelus, hence resulting in a new combination, Zelus couturieri (Bérenger, 2003) comb. nov. Lectotypes, paralectotypes or neotypes are designated for a number of species. Habitus images, illustrations of male genitalia, distribution maps and measurements are provided for nearly all species. The three previously recognized subgenera of Zelus are found to be based upon superficial characters and these divisions do not reflect natural groupings. Using sets of characters, especially those of the male genitalia, eleven species groups are proposed. It is also hypothesized that Zelus is closely related to three other New World genera: Atopozelus Elkins, Ischnoclopius Stål and an undescribed genus "Hartzelus" [manuscript name]. Zelus is endemic to the New World, occurring naturally in the Caribbean and all but one of the continental countries, with introductions to Pacific islands, Europe and Chile.

Project description:Assassin bugs (Hemiptera: Heteroptera: Reduviidae) are venomous insects that prey on invertebrates. Assassin bug venom has features in common with venoms from other animals, such as paralysing and lethal activity when injected, and a molecular composition that includes disulfide-rich peptide neurotoxins. Uniquely, this venom also has strong liquefying activity that has been hypothesised to facilitate feeding through the narrow channel of the proboscis—a structure inherited from sap- and phloem-feeding phytophagous hemipterans and adapted during the evolution of Heteroptera into a fang and feeding structure. However, further understanding of the function of assassin bug venom is impeded by the lack of proteomic studies detailing its molecular composition. In addition, the lack of knowledge regarding venoms of predaceous reduviids limits our understanding of how the venoms of the blood-feeding kissing bugs (Reduviidae: Triatominae) evolved to facilitate hematophagy. By using a combined transcriptomic/proteomic approach we show that the venom proteome of the harpactorine assassin bug Pristhesancus plagipennis includes a complex suite of >100 proteins comprising disulfide-rich peptides, CUB-domain proteins, cystatins, putative cytolytic toxins, triabin-like protein, odorant binding protein, serine proteases, catabolic enzymes, putative nutrient-binding proteins, plus eight families of proteins without homology to characterised proteins. Serine proteases, CUB domain proteins and other novel proteins in the 10–16 kDa mass range, as well as putative cytolytic toxins, were the most abundant venom components. Thus, in addition to putative neurotoxins, assassin bug venom includes a high proportion of enzymatic and cytolytic venom components well suited to tissue liquefaction. While some protein families such as lipocalin/triabins occur in the venoms of both predaceous and blood-feeding reduviids, the composition of venoms in these two groups differs markedly. These results provide insights into the venom evolution in the insect suborder Heteroptera.

Dataset Information

Melt With This Kiss: Paralyzing and Liquefying Venom of The Assassin Bug Pristhesancus plagipennis (Hemiptera: Reduviidae).

Publications

Melt With This Kiss: Paralyzing and Liquefying Venom of The Assassin Bug <i>Pristhesancus plagipennis</i> (Hemiptera: Reduviidae).

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