Venom proteome of two parasitoid wasps, Theocolax elegans and Anisopteromalus calandrae
Ontology highlight
ABSTRACT:
ORGANISM(S): Theocolax Elegans Anisopteromalus Calandrae
SUBMITTER: 
Gongyin Ye
PROVIDER: PXD036002 | iProX | Fri Aug 12 00:00:00 BST 2022
REPOSITORIES: iProX
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Project description:Parasitoid wasps inject venom containing complex bioactive compounds to regulate the immune response and development of host arthropods and sometime paralyze host arthropods. Although extensive studies have been conducted on the identification of venom proteins in larval parasitoids, relatively few studies have examined the pupal parasitoids. Hereby, proteomic method was used to identify putative venom proteins from P. vindemmiae, an ectoparasitoid of Drosophila.
2019-09-27 | PXD015627 | iProX
Project description:Background The generalist dipteran pupal parasitoid Nasonia vitripennis injects 79 venom peptides into the host before egg laying. This venom induces several important changes in the host, including developmental arrest, immunosuppression, and alterations to normal metabolism. It is hoped that diverse and potent bioactivities of N. vitripennis venom provide an opportunity for the design of novel acting drugs. However, currently very little is known about the individual functions of N. vitripennis venom peptides and less than half can be bioinformatically annotated. The paucity of annotation information complicates the design of studies that seek to better understand the potential mechanisms underlying the envenomation response. Although the RNA interference system of N. vitripennis provides an opportunity to functionally characterise venom encoding genes, with 79 candidates this represents a daunting task. For this reason we were interested in determining the expression levels of venom encoding genes in the venom gland, such that this information could be used to rank candidate venoms. To do this we carried out deep sequencing of the transcriptome of the venom gland and neighbouring ovary tissue and used RNA-seq to measure expression from the 79 venom encoding genes. The generation of a specific venom gland transcriptome dataset also provides further opportunities to investigate novel features of this highly specialised organ. Results High throughput sequencing and RNA-seq revealed that the highest expressed venom encoding gene in the venom gland was a serine protease called Nasvi2EG007167, which has previously been implicated in the apoptotic activity of N. vitripennis venom. As expected the RNA-seq confirmed that the N. vitripennis venom encoding genes are almost exclusively expressed in the venom gland relative to the neighbouring ovary tissue. Novel peptides appear to perform key roles in N. vitripennis venom function as only four of the highest 15 expressed venom encoding genes are bioinformatically annotationed. The high throughput sequencing data also provided evidence for the existence of an additional 471 novel genes in the Nasonia genome that are expressed in the venom gland and ovary. Finally, metagenomic analysis of venom gland transcripts identified viral transcripts that may play an important part in the N. vitripennis venom function. Conclusions The expression level information provided here for the 79 venom encoding genes provides an unbiased dataset that can be used by the N. vitripennis community to identify high value candidates for further functional characterisation. These candidates represent bioactive peptides that have value in drug development pipelines.
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Project description:Entomopathogenic nematodes (EPNs) are unique parasitic nematodes due to their symbiosis with entomopathogenic bacteria and their ability to kill insect hosts quickly after infection. Although it has been widely believed that EPNs rely on their bacterial partners for killing insect hosts, compelling evidence from previous studies challenges this model. We developed an improved method of activating millions of Steinernema carpocapsae infective juveniles (IJs) in vitro to harvest excreted/secreted (ES) proteins for bioactivity tests and proteomics analysis. We found that a low dose of the ES proteins from early activated nematodes is lethal to Drosophila melanogaster adults within 2-6 hours. We analyzed the protein composition of this venom using mass spectrometry and identified 472 proteins. Many of these venom proteins share high homology with those of vertebrate-parasitic nematodes. Among many different families of proteins found in the venom, proteases and protease inhibitors are especially abundant. Some toxin-related proteins such as Shk domain-containing proteins were also detected. We further analyzed the transcriptomes of individual non-activated IJs and nematodes that were activated in vitro and in vivo, which revealed a dramatic shift in gene expression during IJ activation. By comparing the whole transcriptomes and the genes encoding venom proteins between the in vitro and in vivo activated nematodes, we confirmed that the in vitro activation is a good approximation of the in vivo process. In summary, our findings strongly support a new model that S. carpocapsae and likely other Steinernema EPNs have a more active role in contributing to the pathogenicity of the nematode-bacterium complex than simply relying on their symbiotic bacteria. Furthermore, we propose that EPNs are a good model system for investigating vertebrate- and human-parasitic nematodes, especially regarding the function of ES products.
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Project description:Insects mount an innate immune response to defend against the foreign invading microorganisms and parasites. To be successful parasites, endoparasitoid wasps need to be able to suppress the immune responses of their hosts. This allows the wasp eggs to hatch and the larvae to develop inside the host. However, the molecular mechanism underlying the interaction between wasp and its host remains largely unknown. In this study, we identified the reprolysin type metalloprotease venom component MmV189, which was designated venom regulatory factor-1 (VRF1). VRF1 plays a critical role in the interaction between the wasp Microplitis mediator and its lepidopteran host Helicoverpa armigera (the cotton bollworm). Proteomics analysis based on isobaric tags for relative and absolute quantitation (iTRAQ) revealed that at least twelve wasp venom proteins were released into the host hemolymph, causing significant changes in 511 host proteins at 24 h post parasitization. Taking an approach of integrated transcriptome and proteome analysis, we identified 313 putative proteins from the wasp venom reservoirs, 25 of which belong to the family of metalloproteases. Proenzyme of VRF1 was firstly cleaved in the host hemolymph after parasitization and then entered the hemocytes. Additionally, depletion of VRF1 in M. mediator by dsRNA-mediated knockdown significantly reduced the percentage of cocoon formation. Furthermore, we showed possible binding of VRF1 to Dorsal, a H. armigera nuclear factor kappa B (NF-κB), using yeast two-hybrid and pull-down assays, and confirmed the cleavage of Dorsal by VRF1. Moreover, we found that VRF1 acts as a protease to process Dorsal in the host hemocytes and suppress the induction of antimicrobial peptides (AMPs). Taken together, our findings identify a novel mechanism by which a component of endoparasitoid wasp venom interferes with host immune signaling cascades.
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