Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1097249 | ENA |
REPOSITORIES: ENA
Similar Datasets
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.
2019-01-07 | PXD007905 | Pride
Project description:A chromosome-level genome assembly of the parasitoid wasp, Cotesia glomerata (Hymenoptera: Braconidae)
| PRJEB45226 | ENA
Project description:Cullin-RING ubiquitin ligases (CRLs) control the degradation of a wide landscape of human proteins in combination with ubiquitin-carrying enzymes (UCEs). CRL expansion during evolution is apparent, with a few dozen in yeast that function with a single UCE and as many as 300 in humans that function with at least 8 UCEs. A major unaddressed question is why human CRL buildup has been accompanied by additional UCEs that function with CRLs. Here we demonstrate that human CRLs and UCEs can display specificity, resulting in increased affinity for each other and enhanced rates of ubiquitin transfer to substrates. To uncover the structural basis for CRL-UCE specificity, cryo-EM was performed on a CRL2 subfamily member with substrate receptor subunit FEM1C (CRL2FEM1C) in complex with a proxy for catalytically active UCE. The structure elucidated an extensive CRL-UCE interface that promotes proximity between the UCE active site and CRL2FEM1C-bound substrate. Unanticipated selectivity was also observed between the CRL substrate Lys ubiquitylation sites and the identity of the UCE. CRL-UCE specificity also manifests during targeted protein degradation by affecting the activities of drugs that induce ubiquitylation of neosubstrates. An emerging CRL code is revealed that drives selective formation of CRL-UCE complexes to promote rapid substrate ubiquitylation.
2024-05-22 | PXD043523 | Pride