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Open AccessArticle

Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus

1
Institute for Insect Biotechnology, Justus-Liebig-Universität Gießen, Heinrich Buff Ring 26–32, 35392 Gießen, Germany
2
LOEWE Centre for Translational Biodiversity Genomics (LOEWE-TBG), Senckenberganlage 25, 60325 Frankfurt, Germany
3
Branch Bioressources, Department Animal Venomics, Fraunhofer Institute for Molecular Biology and Applied Ecology, Ohlebergsweg 12, 35392 Giessen, Germany
4
Protein Analytics, Institute of Biochemistry, Justus-Liebig-Universität Gießen, Friedrichstrasse 24, 35392 Gießen, Germany
5
Institute for Evolutionary Biology and Ecology, Rheinische Friedrich-Wilhelms-Universität Bonn, An der Immenburg 1, 53121 Bonn, Germany
6
Biodiversity and Climate Research Centre, Senckenberg Gesellschaft für Naturforschung, Senckenberganlage 25, 60325 Frankfurt am Main, Germany
*
Author to whom correspondence should be addressed.
Mar. Drugs 2020, 18(8), 407; https://doi.org/10.3390/md18080407
Received: 25 June 2020 / Revised: 20 July 2020 / Accepted: 27 July 2020 / Published: 1 August 2020
Nemerteans (ribbon worms) employ toxins to subdue their prey, but research thus far has focused on the small-molecule components of mucus secretions and few protein toxins have been characterized. We carried out a preliminary proteotranscriptomic analysis of putative toxins produced by the hoplonemertean Amphiporus lactifloreus (Hoplonemertea, Amphiporidae). No variants were found of known nemertean-specific toxin proteins (neurotoxins, cytotoxins, parbolysins or nemertides) but several toxin-like transcripts were discovered, expressed strongly in the proboscis, including putative metalloproteinases and sequences resembling sea anemone actitoxins, crown-of-thorn sea star plancitoxins, and multiple classes of inhibitor cystine knot/knottin family proteins. Some of these products were also directly identified in the mucus proteome, supporting their preliminary identification as secreted toxin components. Two new nemertean-typical toxin candidates could be described and were named U-nemertotoxin-1 and U-nemertotoxin-2. Our findings provide insight into the largely overlooked venom system of nemerteans and support a hypothesis in which the nemertean proboscis evolved in several steps from a flesh-melting organ in scavenging nemerteans to a flesh-melting and toxin-secreting venom apparatus in hunting hoplonemerteans. View Full-Text
Keywords: nemertean toxins; transcriptomics; proteomics; inhibitor cystine knot/knottin; actitoxins; plancitoxins; nemertotoxins; hoplonemerteans nemertean toxins; transcriptomics; proteomics; inhibitor cystine knot/knottin; actitoxins; plancitoxins; nemertotoxins; hoplonemerteans
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  • Supplementary File 1:

    ZIP-Document (ZIP, 262 KiB)

  • Externally hosted supplementary file 1
    Doi: 10.5281/zenodo.3908343
    Link: https://zenodo.org/deposit/3908343
    Description: Additional data is provided in the open access database ZENODO: https://zenodo.org/ with the DOI: 10.5281/zenodo.3908343. Additional file1: BLASTP database of known nemertean toxins, Additional file2: Alignment of matching nemertide sequences from N. genicularis, Additional file3: Alignment of matching parbolysin sequences from N. geniculatus, Additional file4: Mascot-based result table of the epidermis proteome sequences, Additional file5: Mascot-based result table of the mucus proteome sequences, Additional file6: Used Illumina adapter-file, Additional file7: Assembly file of A. lactifloreus, Additional file8: Assembly file of N. geniculatus, Additional file9: Transdecoder file with predicted ORFs for A. lactifloreus, Additional file10: Transdecoder file with predicted ORFs for N. geniculatus, Additional file11: BLASTP database of SwissProt, Additional file12: BLASTP database of ToxProt, Additional file13: BLASTP database of antimicrobial peptides, Additional file14: BLASTP results against known nemertean toxins for A. lactifloreus, Additional file15: BLASTP results against known nemertean toxins for N. geniculatus, Additional file16: BLASTP results against SwissProt for A. lactifloreus, Additional file17: BLASTP results against SwissProt for N. geniculatus, Additional file18: BLASTP results against ToxProt for A. lactifloreus, Additional file19: BLASTP results against ToxProt for N. genicularis, Additional file20: BLASTP results against AMP database for A. lactifloreus, Additional file21: BLASTP results against AMP database for N. geniculatus, Additional file 22: Zip.file with all alignments of transcriptome-wise identified putative toxins, Additional file 23: Zip.file with all alignments of proteome-wise identified putative toxins.
  • Externally hosted supplementary file 2
    Doi: doi:10.5281/zenodo.3908343
    Link: https://zenodo.org/record/3908343
    Description: Additional data are provided in the open access database ZENODO
MDPI and ACS Style

von Reumont, B.M.; Lüddecke, T.; Timm, T.; Lochnit, G.; Vilcinskas, A.; von Döhren, J.; Nilsson, M.A. Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus. Mar. Drugs 2020, 18, 407. https://doi.org/10.3390/md18080407

AMA Style

von Reumont BM, Lüddecke T, Timm T, Lochnit G, Vilcinskas A, von Döhren J, Nilsson MA. Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus. Marine Drugs. 2020; 18(8):407. https://doi.org/10.3390/md18080407

Chicago/Turabian Style

von Reumont, Björn M.; Lüddecke, Tim; Timm, Thomas; Lochnit, Günter; Vilcinskas, Andreas; von Döhren, Jörn; Nilsson, Maria A. 2020. "Proteo-Transcriptomic Analysis Identifies Potential Novel Toxins Secreted by the Predatory, Prey-Piercing Ribbon Worm Amphiporus lactifloreus" Mar. Drugs 18, no. 8: 407. https://doi.org/10.3390/md18080407

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