(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Paraneoptera: NE > Hemiptera: NE > Prosorrhyncha: NE > Heteroptera: NE > Euheteroptera: NE > Neoheteroptera: NE > Panheteroptera: NE > Cimicomorpha: NE > Reduvioidea: NE > Reduviidae: NE > Harpactorinae: NE > Harpactorini: NE > Pristhesancus: NE > Pristhesancus plagipennis: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MDYFNINIYLVFIWLILLESFGHCSVTLYRKAKCSVPKDIDHVKRSSLFE ECISKKYDIGKKTPCYDQLGCFPRNGSWVNLLRPFPSPFPPEDIETGIKL YTRKNLEGYTVRLWPEINLKGSDFKPKRAATVIVTHGFSSNGNADWLMEL KNVYLEKIDANVFIVDWGEGAKLLNYLQVASNTRIVGAELVRFGKHLVGL GLHPDKIHLIGHSLGAHIMAYMAKGIQSPSKIRRITALDPAQPGFEGTSK KVKLTKGDAKYIDVIHTNAKPLIPFLGFGLMAPAGDVDFYMNGGTTQPGC LLDIKIPKITSILDLATMAVEAISQWISCSHSRAYEYFIWSLKQPDCLMI GRKMTMIENILKIKTLGILGVFDPIVKKLDQCRLKTCTVLGLKTFKLSAR GAFAVVTKPLEPYCDTPKDVMKLFGKLIKGLENLIAGTIGKIT
Reference
Title: Melt With This Kiss: Paralyzing and Liquefying Venom of The Assassin Bug Pristhesancus plagipennis (Hemiptera: Reduviidae) Walker AA, Madio B, Jin J, Undheim EA, Fry BG, King GF Ref: Mol Cell Proteomics, 16:552, 2017 : PubMed
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.
