Abstract
Sea anemones produce pore-forming toxins, actinoporins, which are interesting as tools for cytoplasmic membranes study, as well as being potential therapeutic agents for cancer therapy. This investigation is devoted to structural and functional study of the Heteractis crispa actinoporins diversity. Here, we described a multigene family consisting of 47 representatives expressed in the sea anemone tentacles as prepropeptide-coding transcripts. The phylogenetic analysis revealed that actinoporin clustering is consistent with the division of sea anemones into superfamilies and families. The transcriptomes of both H. crispa and Heteractis magnifica appear to contain a large repertoire of similar genes representing a rapid expansion of the actinoporin family due to gene duplication and sequence divergence. The presence of the most abundant specific group of actinoporins in H. crispa is the major difference between these species. The functional analysis of six recombinant actinoporins revealed that H. crispa actinoporin grouping was consistent with the different hemolytic activity of their representatives. According to molecular modeling data, we assume that the direction of the N-terminal dipole moment tightly reflects the actinoporins’ ability to possess hemolytic activity.
Highlights
Actinoporins are biologically active polypeptides (17–20 kDa) that are found in sea anemones [1,2,3,4,5].Their structure includes compact β-fold, without disulfide bonds, formed by 12 β-sheets and two α-helices, one of which, functional and more extended, is located at the N-terminus, and the second one, short, is at the C-terminus [5]
The results indicate that H. crispa actinoporins are encoded by the multigene family containing of 47 representatives at least
We have performed a comprehensive investigation of H. crispa actinoporins, including molecular cloning, modeling, and biological activity testing
Summary
Actinoporins are biologically active polypeptides (17–20 kDa) that are found in sea anemones [1,2,3,4,5]. Their structure includes compact β-fold, without disulfide bonds, formed by 12 β-sheets and two α-helices, one of which, functional and more extended, is located at the N-terminus, and the second one, short, is at the C-terminus [5]. 165–179 amino acids and are comprised together with actinoporin-like proteins and fungal fruit-body lectin family into the superfamily of membrane binding proteins, called AF domains [6].
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
