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Polypeptides secreted from the columnar vesicles of the sea anemone Bunodosoma cangicum and their in vivo effects on Caenorhabditis elegans
Author(s) -
Bastos Claudio L.Q.,
Josende Marcelo Estrella,
Ferreira Shana Pires,
de Magalhães Mariana Torquato Quezado,
de Castro Pimenta Adriano Monteiro,
Lima Juliane Ventura,
Boyle Robert Tew
Publication year - 2019
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.11107
Subject(s) - sea anemone , caenorhabditis elegans , in vivo , biology , size exclusion chromatography , peptide , vesicle , anemone , mass spectrometry , microbiology and biotechnology , biochemistry , chemistry , chromatography , botany , membrane , genetics , enzyme , gene
In this study we provide new evidence that the columnar vesicles of the sea anemone Bunodosoma cangicum are toxic in vivo and contain at least two active polypeptides, a neurotoxic and an apoptosis inducing polypeptide. Here we show that it is also an effective inducer of apoptosis in vivo in the nematode Caenorhabditis elegans . In addition, the anemone peptides rapidly paralyze C. elegans , and set in motion a sequence of events that result in the complete dissolution of the internal organs in adult animals within 60 min. Nematodes that survive the toxin treatment exhibit a decreased reproductive capacity. Interestingly, adult animals appear to be much more susceptible to the effects of the toxins than larval stages, suggesting possible developmentally dependent targets of the toxins. Here we also provide chemical characterization of the compounds through chromatographic analysis and mass spectrometry. Gel filtration chromatography coupled with reverse phase HPLC shows that our partially purified extract contains at least two principle components. Additionally, MALDI‐TOF mass spectrometry analysis of our extract shows three principal compounds at 814.6, 2914.1, and 4360.3 m/z plus three other minor components or fragments. Mass spectrometry analysis also indicates the presence of three disulfide bridges. Which is in agreement with other characterizations of anemone venoms.