Venomous globiferous pedicellariae of eastern Australian Tripneustes sea urchins contain a rich diversity of cathepsin, lectin, and phospholipase A2 family proteins

Sea urchins (Echinoidea) are a class of echinoderms that are known to harbour diverse defensive traits, including long spines and pincer-like appendages called pedicellariae. Pedicellariae of the venomous globiferous type are particularly well developed in the Family Toxopneustidae. However, there is a significant lack of data on the identity of pedicellarial toxins, which is needed to characterise their function, generate insights into venom evolution and explore bioprospecting potential. In this study, we performed a transcriptomic assessment of the pedicellariae from the two toxopneustid Tripneustes species that occur in eastern Australia, both of which are suspected to possess a pedicellarial venom gland system. The pedicellariae were found to express a rich diversity of gene transcripts encoding proteins that match to known putative venom-associated proteins, particularly those of cathepsin, lectin, and phospholipase A<sub>2</sub> families. This study provides a foundational basis to advance discovery of sea urchin venom toxin candidates, filling a void in a field of research that has been neglected.

Authors

Institutions

Publication Details

Journal
Toxicon
Published
2026-03-12
DOI
https://doi.org/10.1016/j.toxicon.2026.109062
Citations
1
Primary Topic
Marine Invertebrate Physiology and Ecology
Type
article
Field-Weighted Citation Impact
43.71
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Venomous globiferous pedicellariae of eastern Australian Tripneustes sea urchins contain a rich diversity of cathepsin, lectin, and phospholipase A2 family proteins

Cherie A. Motti, Richard J. Harris, Scott F. Cummins, Sina Ehlert-Flaskämper et al.
1 citations
Toxicon
Marine Invertebrate Physiology and Ecology
43.71
article

Venomous globiferous pedicellariae of eastern Australian Tripneustes sea urchins contain a rich diversity of cathepsin, lectin, and phospholipase A2 family proteins

Cherie A. Motti, Richard J. Harris, Scott F. Cummins, Sina Ehlert-Flaskämper, Maria Byrne
article en
1 citations

Abstract

Sea urchins (Echinoidea) are a class of echinoderms that are known to harbour diverse defensive traits, including long spines and pincer-like appendages called pedicellariae. Pedicellariae of the venomous globiferous type are particularly well developed in the Family Toxopneustidae. However, there is a significant lack of data on the identity of pedicellarial toxins, which is needed to characterise their function, generate insights into venom evolution and explore bioprospecting potential. In this study, we performed a transcriptomic assessment of the pedicellariae from the two toxopneustid Tripneustes species that occur in eastern Australia, both of which are suspected to possess a pedicellarial venom gland system. The pedicellariae were found to express a rich diversity of gene transcripts encoding proteins that match to known putative venom-associated proteins, particularly those of cathepsin, lectin, and phospholipase A<sub>2</sub> families. This study provides a foundational basis to advance discovery of sea urchin venom toxin candidates, filling a void in a field of research that has been neglected.

ToxiconVol. 276
University of the Sunshine Coast (AU), Australian Institute of Tropical Health and Medicine (AU), Sydney Institute of Marine Science (AU), James Cook University (AU)
Life below water
Openalex Percentile: Top 0%
Marine Invertebrate Physiology and Ecology
43.71
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.