A Comparative Analysis of the Venom System Between Two Morphotypes of the Sea Anemone

Overview

Journal Animals (Basel)

Date 2024 Mar 28

PMID 38540078

Authors

Maria Alcaide

Ines Moutinho Cabral

Lara Carvalho

Vera M Mendes

Antonio P Alves de Matos

Bruno Manadas

Leonor Saude

Mariaelena DAmbrosio

Pedro M Costa

Affiliations

Soon will be listed here.

Abstract

The current study investigates the venom-delivery system of green and red morphotypes of the sea anemone to disclose its potential as a source of bioactive compounds. We compared the two morphotypes using electron and optical microscopy, proteomics, and toxicity assessment on zebrafish embryos. Specialized venom-injecting cells (nematocysts) are equally distributed and found in the tentacles of both varieties. Proteomics revealed proteins of interest in both red and green , yielding the three most abundant Gene Ontology (GO) terms related to the biological processes "proteolysis", "hemolysis in another organism" and "lipid catabolic process". Neurotoxins and cytolytic toxins similar to known cnidarian toxins like PsTX-60A and AvTX-60A, for instance, were identified in both types. Extracts from green and red anemones were toxic to zebrafish embryos, with green anemone venom appearing to be more potent. The findings highlight the presence of proteinaceous toxins in and the potential for different varieties to possess distinct bioactive compounds. Notably, pore-forming toxins are suggested for molecular probes and immunotoxins, making them valuable assets for potential biotechnological and biomedical purposes.

References

Ramirez-Carreto S, Miranda-Zaragoza B, Rodriguez-Almazan C . Actinoporins: From the Structure and Function to the Generation of Biotechnological and Therapeutic Tools. Biomolecules. 2020; 10(4). PMC: 7226409. DOI: 10.3390/biom10040539. View

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

Bradford M . A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976; 72:248-54. DOI: 10.1016/0003-2697(76)90527-3. View

Williams J, Day M, Heavner J . Ziconotide: an update and review. Expert Opin Pharmacother. 2008; 9(9):1575-83. DOI: 10.1517/14656566.9.9.1575. View

Jouiaei M, Yanagihara A, Madio B, Nevalainen T, Alewood P, Fry B . Ancient Venom Systems: A Review on Cnidaria Toxins. Toxins (Basel). 2015; 7(6):2251-71. PMC: 4488701. DOI: 10.3390/toxins7062251. View

Frazao B, Vasconcelos V, Antunes A . Sea anemone (Cnidaria, Anthozoa, Actiniaria) toxins: an overview. Mar Drugs. 2012; 10(8):1812-1851. PMC: 3447340. DOI: 10.3390/md10081812. View

Oshiro N, Kobayashi C, Iwanaga S, Nozaki M, Namikoshi M, Spring J . A new membrane-attack complex/perforin (MACPF) domain lethal toxin from the nematocyst venom of the Okinawan sea anemone Actineria villosa. Toxicon. 2004; 43(2):225-8. DOI: 10.1016/j.toxicon.2003.11.017. View

Inoue T, Osatake H . A new drying method of biological specimens for scanning electron microscopy: the t-butyl alcohol freeze-drying method. Arch Histol Cytol. 1988; 51(1):53-9. DOI: 10.1679/aohc.51.53. View

Sher D, Fishman Y, Zhang M, Lebendiker M, Gaathon A, Mancheno J . Hydralysins, a new category of beta-pore-forming toxins in cnidaria. J Biol Chem. 2005; 280(24):22847-55. DOI: 10.1074/jbc.M503242200. View

10.

Upadhyay S, Eckel-Mahan K, Mirbolooki M, Tjong I, Griffey S, Schmunk G . Selective Kv1.3 channel blocker as therapeutic for obesity and insulin resistance. Proc Natl Acad Sci U S A. 2013; 110(24):E2239-48. PMC: 3683782. DOI: 10.1073/pnas.1221206110. View

11.

VENABLE J, COGGESHALL R . A SIMPLIFIED LEAD CITRATE STAIN FOR USE IN ELECTRON MICROSCOPY. J Cell Biol. 1965; 25:407-8. PMC: 2106628. DOI: 10.1083/jcb.25.2.407. View

12.

Nagai H, Oshiro N, Takuwa-Kuroda K, Iwanaga S, Nozaki M, Nakajima T . Novel proteinaceous toxins from the nematocyst venom of the Okinawan sea anemone Phyllodiscus semoni Kwietniewski. Biochem Biophys Res Commun. 2002; 294(4):760-3. DOI: 10.1016/S0006-291X(02)00547-8. View

13.

Christinat A, Leyvraz S . Role of trabectedin in the treatment of soft tissue sarcoma. Onco Targets Ther. 2010; 2:105-13. PMC: 2886331. DOI: 10.2147/ott.s4454. View

14.

de Castro Figueiredo Bordon K, Cologna C, Fornari-Baldo E, Pinheiro-Junior E, Cerni F, Amorim F . From Animal Poisons and Venoms to Medicines: Achievements, Challenges and Perspectives in Drug Discovery. Front Pharmacol. 2020; 11:1132. PMC: 7396678. DOI: 10.3389/fphar.2020.01132. View

15.

Beeton C, Pennington M, Wulff H, Singh S, Nugent D, Crossley G . Targeting effector memory T cells with a selective peptide inhibitor of Kv1.3 channels for therapy of autoimmune diseases. Mol Pharmacol. 2005; 67(4):1369-81. PMC: 4275123. DOI: 10.1124/mol.104.008193. View

16.

Menezes C, Thakur N . Sea anemone venom: Ecological interactions and bioactive potential. Toxicon. 2022; 208:31-46. DOI: 10.1016/j.toxicon.2022.01.004. View

17.

Nisa S, Vinu D, Krupakar P, Govindaraju K, Sharma D, Vivek R . Jellyfish venom proteins and their pharmacological potentials: A review. Int J Biol Macromol. 2021; 176:424-436. DOI: 10.1016/j.ijbiomac.2021.02.074. View

18.

Stabili L, Schirosi R, Parisi M, Piraino S, Cammarata M . The Mucus of Actinia equina (Anthozoa, Cnidaria): An Unexplored Resource for Potential Applicative Purposes. Mar Drugs. 2015; 13(8):5276-96. PMC: 4557023. DOI: 10.3390/md13085276. View

19.

Sahyoun C, Krezel W, Mattei C, Sabatier J, Legros C, Fajloun Z . Neuro- and Cardiovascular Activities of Snake Venom. Biology (Basel). 2022; 11(6). PMC: 9219918. DOI: 10.3390/biology11060888. View

20.

Rocha J, Peixe L, Gomes N, Calado R . Cnidarians as a source of new marine bioactive compounds--an overview of the last decade and future steps for bioprospecting. Mar Drugs. 2011; 9(10):1860-1886. PMC: 3210609. DOI: 10.3390/md9101860. View