ArticlePloS one2012
Venom proteome of the box jellyfish Chironex fleckeri.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.
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Who cites it
27 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.
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- Sea anemone Bartholomea annulata venom inhibits voltage-gated NaScientific reports · 2022Article
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- Cloning and Expression of N-CFTX-1 Antigen fromIranian journal of public health · 2021Article
- The cnidarian parasitePeerJ · 2021Article
- Advances in venomics: Modern separation techniques and mass spectrometry.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020Review
- A Review of Toxins from Cnidaria.Marine drugs · 2020Review
- Biotechnological Applications of Scyphomedusae.Marine drugs · 2019Review
- A genome wide survey reveals multiple nematocyst-specific genes in Myxozoa.BMC evolutionary biology · 2018Article
- Structural Characterisation of Predicted Helical Regions in theMarine drugs · 2018Article
- Functional and proteomic analysis of Ceratonova shasta (Cnidaria: Myxozoa) polar capsules reveals adaptations to parasitism.Scientific reports · 2017Article
- Analysis of Pelagia noctiluca proteome Reveals a Red Fluorescent Protein, a Zinc Metalloproteinase and a Peroxiredoxin.The protein journal · 2017Article
- High-throughput expression of animal venom toxins in Escherichia coli to generate a large library of oxidized disulphide-reticulated peptides for drug discovery.Microbial cell factories · 2017Article
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- Jellyfish Bioactive Compounds: Methods for Wet-Lab Work.Marine drugs · 2016Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nematocyst is a complex intracellular structure unique to Cnidaria. When triggered to discharge, the nematocyst explosively releases a long spiny, tubule that delivers an often highly venomous mixture of components. The box jellyfish, Chironex fleckeri, produces exceptionally potent and rapid-acting venom and its stings to humans cause severe localized and systemic effects that are potentially life-threatening. In an effort to identify toxins that could be responsible for the serious health effects caused by C. fleckeri and related species, we used a proteomic approach to profile the protein components of C. fleckeri venom. Collectively, 61 proteins were identified, including toxins and proteins important for nematocyte development and nematocyst formation (nematogenesis). The most abundant toxins identified were isoforms of a taxonomically restricted family of potent cnidarian proteins. These toxins are associated with cytolytic, nociceptive, inflammatory, dermonecrotic and lethal properties and expansion of this important protein family goes some way to explaining the destructive and potentially fatal effects of C. fleckeri venom. Venom proteins and their post-translational modifications (PTMs) were further characterized using toxin-specific antibodies and phosphoprotein/glycoprotein-specific stains. Results indicated that glycosylation is a common PTM of the toxin family while a lack of cross-reactivity by toxin-specific antibodies infers there is significant divergence in structure and possibly function among family members. This study provides insight into the depth and diversity of protein toxins produced by harmful box jellyfish and represents the first description of a cubozoan jellyfish venom proteome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.