Psytalla horrida transcriptomics
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB36336 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR3833755_1.fastq.gz | Fastqsanger.gz | |||
| ERR3833755_2.fastq.gz | Fastqsanger.gz | |||
| ERR3833756_1.fastq.gz | Fastqsanger.gz | |||
| ERR3833756_2.fastq.gz | Fastqsanger.gz | |||
| ERR3833757_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 8 |
Similar Datasets
Project description:Venom used for defense, overwhelming and digesting prey in two Reduviid assassin bugs, Platymeris biguttatus and Psytalla horrida
| PRJEB36335 | ENA
Project description:Assassin bugs are one of the diversified groups of venomous predatory insects. Their venom is secreted from three different lumens of salivary gland and can lead to paralysis, lethality and liquidation of the prey, respectively. Nevertheless, the venom components responsible for these effects are not clear. In this study, we use transcriptomics and proteomics to determine the effective salivary protein components in the separate lumen of salivary gland from the assassin bug Platymeris biguttatus, and to conduct toxicological analysis on the function of the salivary gland compartments. Our study sheds light on the functional cooperation between different salivary gland lumens of assassin bugs, and will further the understanding of physiological adaptations of venom-based predation and defense in venomous insects
2022-02-06 | PXD031473 |
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.
2017-11-14 | PXD004804 | Pride
Project description:We found that assassin bugs from the earliest-diverging subfamily of higher Reduviidae (Peiratinae), as well as a subfamily closely related to Triatominae (Stenopodainae) have venom that is highly similar in composition to that produced by previously examined reduviids from Harpactorinae and Reduviinae. This finding suggests that venom composition has been largely stable due to purifying selection among the higher Reduviidae, which is consistent with the ancient origin of venom in the ancestors of Heteroptera 250–300 million years ago (Sunagar and Moran 2015; Walker et al. 2018a). This near homogeneity of venom composition is perhaps surprising considering that reduviid predators have evolved numerous instances of prey specialization and specialized hunting strategies that might be expected to co-evolve with venom. Possibly, further studies focussing on species with more specialized hunting strategies, or different kinds of venom bioactivities, will uncover more nuanced venom adaptations. Alternatively, it is possible that the protease-rich venoms of predatory reduviids are simply well-suited to myriad different hunting strategies. These data are consistent with other examples where venoms are surprisingly similar despite great differences in biology, for example between solitary and eusocial bees. A more detailed picture of venom evolution in Reduviidae would examine venom produced by the early-diverging Phymatine complex as well as venoms of non-reduviid cimicomorphs, prey specialists such as the arachnophagous Emesinae and the myrmecophagous Holoptilinae, and some of the many groups that employ hunting specializations, such as the use of plant resins to catch prey (Hwang and Weirauch 2012). Within Triatominae, examination of saliva produced by additional species from multiple lineages (especially those that switched to blood-feeding independently, if the subfamily is shown to be polyphyletic) and including generalists and specialists on different host taxa and species associated especially with nests and burrows will be informative. The venoms of predatory reduviids such as Zelurus spp. and Opisthacidius spp. that are most closely related to Triatominae, and share some behaviours such as habitation of bird nests by Opisthacidius spp. may also provide more information about the evolution of triatomine saliva.
2024-07-30 | PXD050854 | Pride
Project description:Predatory bugs capture prey by injecting venom from their salivary glands using specialized stylets. Understanding venom function has been impeded by a scarcity of knowledge of their venom composition. We therefore examined the proteinaceous components of the salivary venom of the predatory stink bug Arma chinensis (Hemiptera: Pentatomidae). Using gland extracts and venoms from 5th-instar nymphs or adult females, we performed shotgun proteomics combined with venom gland transcriptomics. We found that the venom of A. chinensis comprised a complex suite of over a hundred individual proteins, including oxidoreductases, transferases, hydrolases, ligases, protease inhibitors, and recognition, transport and binding proteins. Besides the uncharacterized proteins, hydrolases such as venom serine proteases, cathepsins, phospholipase A2, phosphatases, nucleases, alpha-amylases, and chitinases constitute the most abundant protein families. However, salivary proteins shared by and unique to other predatory heteropterans were not detected in A. chinensis venom. Injection of the proteinaceous (> 3 kDa) venom fraction of A. chinensis gland extracts or venom into its prey, the larvae of the Oriental armyworm Mythimna separata (Walker, 1865), revealed insecticidal activity against lepidopterans. Our data expands the knowledge of heteropteran salivary proteins and suggests predatory asopine bugs as a novel source for bioinsecticides.
2023-07-20 | PXD040272 | Pride
Project description:Tilletia horrida isolate TX5 Genome sequencing and assembly
| PRJNA885871 | ENA
Project description:Tilletia horrida isolate TX7 Genome sequencing and assembly
| PRJNA885876 | ENA
Project description:Tilletia horrida isolate TX4 Genome sequencing and assembly
| PRJNA885870 | ENA