Metabolomics,Unknown,Transcriptomics,Genomics,Proteomics

Dataset Information

Deep sequencing of pyrethroid-resistant bed bugs reveals multiple mechanisms of resistance within a single population

ABSTRACT: A frightening resurgence of bed bug infestations has occurred over the last 10 years in the US. Current chemical methods have been inadequate for controlling bed bugs due to widespread insecticide resistance. Little is known about the mechanisms of resistance present in US bed bug populations, making it extremely difficult to develop intelligent strategies to control this pest. We have identified bed bugs collected in Richmond, VA which exhibit both kdr-type (L925I) and metabolic resistance to pyrethroid insecticides. LD50 bioassays determined resistance ratios of ~6000-fold to the insecticide deltamethrin, with contact bioassays confirming cross-resistance to several other labeled formulations. To identify metabolic genes potentially involved in the detoxification of pyrethroids, we performed deep-sequencing of the adult bed bug transcriptome, obtaining more than 2.5 million reads on the 454 titanium platform. Following assembly, analysis of newly identified gene transcripts in both Harlan (susceptible) and Richmond (resistant) bed bugs revealed several candidate cytochrome P450 and carboxyesterase genes which were significantly over-expressed in the resistant strain, consistent with the idea of increased metabolic resistance. These data will accelerate efforts to understand the biochemical basis for insecticide resistance in bed bugs, and provide molecular markers to assist in the surveillance of metabolic resistance. Deep sequencing was performed from total RNA isolated from adult male bed bugs using the Titanium 454 platform

ORGANISM(S): Cimex lectularius

SUBMITTER: Zach Adelman

PROVIDER: E-GEOD-31025 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Publications

Deep sequencing of pyrethroid-resistant bed bugs reveals multiple mechanisms of resistance within a single population.

Adelman Zach N ZN Kilcullen Kathleen A KA Koganemaru Reina R Anderson Michelle A E MA Anderson Troy D TD Miller Dini M DM

PloS one 20111019 10

A frightening resurgence of bed bug infestations has occurred over the last 10 years in the U.S. and current chemical methods have been inadequate for controlling this pest due to widespread insecticide resistance. Little is known about the mechanisms of resistance present in U.S. bed bug populations, making it extremely difficult to develop intelligent strategies for their control. We have identified bed bugs collected in Richmond, VA which exhibit both kdr-type (L925I) and metabolic resistance ...[more]

PMID: 22039447

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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

Deep sequencing of pyrethroid-resistant bed bugs reveals multiple mechanisms of resistance within a single population

Publications

Deep sequencing of pyrethroid-resistant bed bugs reveals multiple mechanisms of resistance within a single population.

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