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Open AccessArticle

Proteo-Transcriptomic Characterization of the Venom from the Endoparasitoid Wasp Pimpla turionellae with Aspects on Its Biology and Evolution

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Project group Bioressources, Animal Venomics, Fraunhofer Institute for Molecular Biology and Applied Ecology, Winchesterstrasse 2, 35392 Giessen, Germany
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Research Group Mass Spectrometry/Proteomics, Max Planck Institute for Chemical Ecology, Hans-Knoell-Strasse 8, 07745 Jena, Germany
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Department of Entomology, Max Planck Institute for Chemical Ecology, Hans-Knoell-Strasse 8, 07745 Jena, Germany
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Protein Analytics, Institute of Biochemistry, Justus Liebig University, Friedrichstrasse 24, 35392 Giessen, Germany
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Bioinformatics Core Facility, Bioinformatics and Systems Biology, Justus Liebig University, Heinrich Buff Ring 58, 35394 Giessen, Germany
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Institute for Insect Biotechnology, Justus Liebig University, Heinrich Buff Ring 58, 35394 Giessen, Germany
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LOEWE Centre for Translational Biodiversity Genomics (LOEWE-TBG), Senckenberganlage 25, 60325 Frankfurt, Germany
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Authors to whom correspondence should be addressed.
Toxins 2019, 11(12), 721; https://doi.org/10.3390/toxins11120721
Received: 19 November 2019 / Revised: 3 December 2019 / Accepted: 7 December 2019 / Published: 10 December 2019
(This article belongs to the Section Animal Venoms)
Within mega-diverse Hymenoptera, non-aculeate parasitic wasps represent 75% of all hymenopteran species. Their ovipositor dual-functionally injects venom and employs eggs into (endoparasitoids) or onto (ectoparasitoids) diverse host species. Few endoparasitoid wasps such as Pimpla turionellae paralyze the host and suppress its immune responses, such as encapsulation and melanization, to guarantee their offspring’s survival. Here, the venom and its possible biology and function of P. turionellae are characterized in comparison to the few existing proteo-transcriptomic analyses on parasitoid wasp venoms. Multiple transcriptome assembly and custom-tailored search and annotation strategies were applied to identify parasitoid venom proteins. To avoid false-positive hits, only transcripts were finally discussed that survived strict filter settings, including the presence in the proteome and higher expression in the venom gland. P. turionella features a venom that is mostly composed of known, typical parasitoid enzymes, cysteine-rich peptides, and other proteins and peptides. Several venom proteins were identified and named, such as pimplin2, 3, and 4. However, the specification of many novel candidates remains difficult, and annotations ambiguous. Interestingly, we do not find pimplin, a paralytic factor in Pimpla hypochondriaca, but instead a new cysteine inhibitor knot (ICK) family (pimplin2), which is highly similar to known, neurotoxic asilid1 sequences from robber flies. View Full-Text
Keywords: hymenopteran venomics; parasitoid wasps; proteomics; transcriptomics; Pimplin2; ICK; knottins hymenopteran venomics; parasitoid wasps; proteomics; transcriptomics; Pimplin2; ICK; knottins
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Özbek, R.; Wielsch, N.; Vogel, H.; Lochnit, G.; Foerster, F.; Vilcinskas, A.; von Reumont, B.M. Proteo-Transcriptomic Characterization of the Venom from the Endoparasitoid Wasp Pimpla turionellae with Aspects on Its Biology and Evolution. Toxins 2019, 11, 721.

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  • Supplementary File 1:

    ZIP-Document (ZIP, 539 KB)

  • Externally hosted supplementary file 1
    Doi: 10.5281/zenodo.3545834
    Link: https://zenodo.org/record/3545834
    Description: Additional data is provided in the open access database ZENODO: https://zenodo.org/record/3545834 Additional data file 1 (RNASeq de novo assembly), Additional data file 2 (Coding regions predicted with Transdecoder), Additional data file 3 (MassSpec mgf file), Additional data file 4 (MassSpec mzML file), Additional data file 5_(MassSpec pkl file, Additional data file 6 (MassSpec raw data), Additional data file 7 (Sequence alignments to train HMMsearch), Additional data file 8 (Sequences to train JACHHMMERSearch), Additional data file 9 (Alignments of known venom proteins), Additional data file 10 (Alignments of novel venom proteins).
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