Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera
Actinoporins are proteinaceous toxins known for their ability to bind to and create pores in cellular membranes. This quality has generated interest in their potential use as new tools, such as therapeutic immunotoxins. Isolated historically from sea anemones, genes encoding for similar actinoporin-...
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-01-01
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| Series: | Marine Drugs |
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| Online Access: | https://www.mdpi.com/1660-3397/20/1/74 |
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| author | Kenneth Sandoval Grace P. McCormack |
| author_facet | Kenneth Sandoval Grace P. McCormack |
| author_sort | Kenneth Sandoval |
| collection | DOAJ |
| description | Actinoporins are proteinaceous toxins known for their ability to bind to and create pores in cellular membranes. This quality has generated interest in their potential use as new tools, such as therapeutic immunotoxins. Isolated historically from sea anemones, genes encoding for similar actinoporin-like proteins have since been found in a small number of other animal phyla. Sequencing and <i>de novo</i> assembly of Irish <i>Haliclona</i> transcriptomes indicated that sponges also possess similar genes. An exhaustive analysis of publicly available sequencing data from other sponges showed that this is a potentially widespread feature of the Porifera. While many sponge proteins possess a sequence similarity of 27.70–59.06% to actinoporins, they show consistency in predicted structure. One gene copy from <i>H. indistincta</i> has significant sequence similarity to sea anemone actinoporins and possesses conserved residues associated with the fundamental roles of sphingomyelin recognition, membrane attachment, oligomerization, and pore formation, indicating that it may be an actinoporin. Phylogenetic analyses indicate frequent gene duplication, no distinct clade for sponge-derived proteins, and a stronger signal towards actinoporins than similar proteins from other phyla. Overall, this study provides evidence that a diverse array of Porifera represents a novel source of actinoporin-like proteins which may have biotechnological and pharmaceutical applications. |
| first_indexed | 2024-03-10T01:04:45Z |
| format | Article |
| id | doaj.art-b3ba25681ece46399d5ffd87e33780e6 |
| institution | Directory Open Access Journal |
| issn | 1660-3397 |
| language | English |
| last_indexed | 2024-03-10T01:04:45Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Marine Drugs |
| spelling | doaj.art-b3ba25681ece46399d5ffd87e33780e62023-11-23T14:28:22ZengMDPI AGMarine Drugs1660-33972022-01-012017410.3390/md20010074Actinoporin-like Proteins Are Widely Distributed in the Phylum PoriferaKenneth Sandoval0Grace P. McCormack1Molecular Evolution and Systematics Laboratory, Zoology, Ryan Institute & School of Natural Sciences, National University of Ireland Galway, 23 University Rd., H91 R8EC Galway, IrelandMolecular Evolution and Systematics Laboratory, Zoology, Ryan Institute & School of Natural Sciences, National University of Ireland Galway, 23 University Rd., H91 R8EC Galway, IrelandActinoporins are proteinaceous toxins known for their ability to bind to and create pores in cellular membranes. This quality has generated interest in their potential use as new tools, such as therapeutic immunotoxins. Isolated historically from sea anemones, genes encoding for similar actinoporin-like proteins have since been found in a small number of other animal phyla. Sequencing and <i>de novo</i> assembly of Irish <i>Haliclona</i> transcriptomes indicated that sponges also possess similar genes. An exhaustive analysis of publicly available sequencing data from other sponges showed that this is a potentially widespread feature of the Porifera. While many sponge proteins possess a sequence similarity of 27.70–59.06% to actinoporins, they show consistency in predicted structure. One gene copy from <i>H. indistincta</i> has significant sequence similarity to sea anemone actinoporins and possesses conserved residues associated with the fundamental roles of sphingomyelin recognition, membrane attachment, oligomerization, and pore formation, indicating that it may be an actinoporin. Phylogenetic analyses indicate frequent gene duplication, no distinct clade for sponge-derived proteins, and a stronger signal towards actinoporins than similar proteins from other phyla. Overall, this study provides evidence that a diverse array of Porifera represents a novel source of actinoporin-like proteins which may have biotechnological and pharmaceutical applications.https://www.mdpi.com/1660-3397/20/1/74Poriferamarine sponge<i>Haliclona</i>transcriptomicsactinoporinspore-forming toxins |
| spellingShingle | Kenneth Sandoval Grace P. McCormack Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera Marine Drugs Porifera marine sponge <i>Haliclona</i> transcriptomics actinoporins pore-forming toxins |
| title | Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera |
| title_full | Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera |
| title_fullStr | Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera |
| title_full_unstemmed | Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera |
| title_short | Actinoporin-like Proteins Are Widely Distributed in the Phylum Porifera |
| title_sort | actinoporin like proteins are widely distributed in the phylum porifera |
| topic | Porifera marine sponge <i>Haliclona</i> transcriptomics actinoporins pore-forming toxins |
| url | https://www.mdpi.com/1660-3397/20/1/74 |
| work_keys_str_mv | AT kennethsandoval actinoporinlikeproteinsarewidelydistributedinthephylumporifera AT gracepmccormack actinoporinlikeproteinsarewidelydistributedinthephylumporifera |