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Structural and functional characterization of sticholysin III: A newly discovered actinoporin within the venom of the sea anemone Stichodactyla helianthus.
Arch Biochem Biophys. 2020 Aug 15; 689:108435.AB

Abstract

Actinoporins are a family of pore-forming toxins produced by sea anemones as part of their venomous cocktail. These proteins remain soluble and stably folded in aqueous solution, but when interacting with sphingomyelin-containing lipid membranes, they become integral oligomeric membrane structures that form a pore permeable to cations, which leads to cell death by osmotic shock. Actinoporins appear as multigenic families within the genome of sea anemones: several genes encoding very similar actinoporins are detected within the same species. The Caribbean Sea anemone Stichodactyla helianthus produces three actinoporins (sticholysins I, II and III; StnI, StnII and StnIII) that differ in their toxic potency. For example, StnII is about four-fold more effective than StnI against sheep erythrocytes in causing hemolysis, and both show synergy. However, StnIII, recently discovered in the S. helianthus transcriptome, has not been characterized so far. Here we describe StnIII's spectroscopic and functional properties and show its potential to interact with the other Stns. StnIII seems to maintain the well-preserved fold of all actinoporins, characterized by a high content of β-sheet, but it is significantly less thermostable. Its functional characterization shows that the critical concentration needed to form active pores is higher than for either StnI or StnII, suggesting differences in behavior when oligomerizing on membrane surfaces. Our results show that StnIII is an interesting and unexpected piece in the puzzle of how this Caribbean Sea anemone species modulates its venomous activity.

Authors+Show Affiliations

Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain; Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland; Department of Biological Sciences, University of Massachusetts Lowell, Lowell, MA, USA.Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain; Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.Department of Biological Sciences, University of Massachusetts Lowell, Lowell, MA, USA.Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland.Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain.Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain. Electronic address: alvaromp@quim.ucm.es.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

32485153

Citation

Rivera-de-Torre, Esperanza, et al. "Structural and Functional Characterization of Sticholysin III: a Newly Discovered Actinoporin Within the Venom of the Sea Anemone Stichodactyla Helianthus." Archives of Biochemistry and Biophysics, vol. 689, 2020, p. 108435.
Rivera-de-Torre E, Palacios-Ortega J, Garb JE, et al. Structural and functional characterization of sticholysin III: A newly discovered actinoporin within the venom of the sea anemone Stichodactyla helianthus. Arch Biochem Biophys. 2020;689:108435.
Rivera-de-Torre, E., Palacios-Ortega, J., Garb, J. E., Slotte, J. P., Gavilanes, J. G., & Martínez-Del-Pozo, Á. (2020). Structural and functional characterization of sticholysin III: A newly discovered actinoporin within the venom of the sea anemone Stichodactyla helianthus. Archives of Biochemistry and Biophysics, 689, 108435. https://doi.org/10.1016/j.abb.2020.108435
Rivera-de-Torre E, et al. Structural and Functional Characterization of Sticholysin III: a Newly Discovered Actinoporin Within the Venom of the Sea Anemone Stichodactyla Helianthus. Arch Biochem Biophys. 2020 Aug 15;689:108435. PubMed PMID: 32485153.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Structural and functional characterization of sticholysin III: A newly discovered actinoporin within the venom of the sea anemone Stichodactyla helianthus. AU - Rivera-de-Torre,Esperanza, AU - Palacios-Ortega,Juan, AU - Garb,Jessica E, AU - Slotte,J Peter, AU - Gavilanes,José G, AU - Martínez-Del-Pozo,Álvaro, Y1 - 2020/05/30/ PY - 2020/04/15/received PY - 2020/05/23/revised PY - 2020/05/25/accepted PY - 2020/6/3/pubmed PY - 2020/6/3/medline PY - 2020/6/3/entrez KW - Equinatoxin KW - Fragaceatoxin KW - Oligomerization KW - Pore-forming-toxin SP - 108435 EP - 108435 JF - Archives of biochemistry and biophysics JO - Arch. Biochem. Biophys. VL - 689 N2 - Actinoporins are a family of pore-forming toxins produced by sea anemones as part of their venomous cocktail. These proteins remain soluble and stably folded in aqueous solution, but when interacting with sphingomyelin-containing lipid membranes, they become integral oligomeric membrane structures that form a pore permeable to cations, which leads to cell death by osmotic shock. Actinoporins appear as multigenic families within the genome of sea anemones: several genes encoding very similar actinoporins are detected within the same species. The Caribbean Sea anemone Stichodactyla helianthus produces three actinoporins (sticholysins I, II and III; StnI, StnII and StnIII) that differ in their toxic potency. For example, StnII is about four-fold more effective than StnI against sheep erythrocytes in causing hemolysis, and both show synergy. However, StnIII, recently discovered in the S. helianthus transcriptome, has not been characterized so far. Here we describe StnIII's spectroscopic and functional properties and show its potential to interact with the other Stns. StnIII seems to maintain the well-preserved fold of all actinoporins, characterized by a high content of β-sheet, but it is significantly less thermostable. Its functional characterization shows that the critical concentration needed to form active pores is higher than for either StnI or StnII, suggesting differences in behavior when oligomerizing on membrane surfaces. Our results show that StnIII is an interesting and unexpected piece in the puzzle of how this Caribbean Sea anemone species modulates its venomous activity. SN - 1096-0384 UR - https://www.unboundmedicine.com/medline/citation/32485153/Structural_and_functional_characterization_of_sticholysin_III:_A_newly_discovered_actinoporin_within_the_venom_of_the_sea_anemone_Stichodactyla_helianthus L2 - https://linkinghub.elsevier.com/retrieve/pii/S0003-9861(20)30444-6 DB - PRIME DP - Unbound Medicine ER -
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