Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i>
The nicotinic acetylcholine receptors (nAChRs) are prototypical ligand-gated ion channels, provide cholinergic signaling, and are modulated by various venom toxins and drugs in addition to neurotransmitters. Here, four APETx-like toxins, including two new toxins, named Hmg 1b-2 Met<sub>ox</...
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| Language: | English |
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MDPI AG
2022-10-01
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| Series: | Toxins |
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| Online Access: | https://www.mdpi.com/2072-6651/14/10/697 |
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| author | Rimma S. Kalina Igor E. Kasheverov Sergey G. Koshelev Oksana V. Sintsova Steve Peigneur Ernesto Lopes Pinheiro-Junior Roman S. Popov Victoria E. Chausova Margarita M. Monastyrnaya Pavel S. Dmitrenok Marina P. Isaeva Jan Tytgat Sergey A. Kozlov Emma P. Kozlovskaya Elena V. Leychenko Irina N. Gladkikh |
| author_facet | Rimma S. Kalina Igor E. Kasheverov Sergey G. Koshelev Oksana V. Sintsova Steve Peigneur Ernesto Lopes Pinheiro-Junior Roman S. Popov Victoria E. Chausova Margarita M. Monastyrnaya Pavel S. Dmitrenok Marina P. Isaeva Jan Tytgat Sergey A. Kozlov Emma P. Kozlovskaya Elena V. Leychenko Irina N. Gladkikh |
| author_sort | Rimma S. Kalina |
| collection | DOAJ |
| description | The nicotinic acetylcholine receptors (nAChRs) are prototypical ligand-gated ion channels, provide cholinergic signaling, and are modulated by various venom toxins and drugs in addition to neurotransmitters. Here, four APETx-like toxins, including two new toxins, named Hmg 1b-2 Met<sub>ox</sub> and Hmg 1b-5, were isolated from the sea anemone <i>Heteractis magnifica</i> and characterized as novel nAChR ligands and acid-sensing ion channel (ASIC) modulators. All peptides competed with radiolabeled α-bungarotoxin for binding to <i>Torpedo californica</i> muscle-type and human α7 nAChRs. Hmg 1b-2 potentiated acetylcholine-elicited current in human α7 receptors expressed in <i>Xenopus laevis</i> oocytes. Moreover, the multigene family coding APETx-like peptides library from <i>H. magnifica</i> was described and in silico surface electrostatic potentials of novel peptides were analyzed. To explain the 100% identity of some peptide isoforms between <i>H. magnifica</i> and <i>H. crispa</i>, 18S rRNA, COI, and ITS analysis were performed. It has been shown that the sea anemones previously identified by morphology as <i>H. crispa</i> belong to the species <i>H. magnifica</i>. |
| first_indexed | 2024-03-09T19:25:27Z |
| format | Article |
| id | doaj.art-f8c7904b69e44bd89b55f55789cdec7a |
| institution | Directory Open Access Journal |
| issn | 2072-6651 |
| language | English |
| last_indexed | 2024-03-09T19:25:27Z |
| publishDate | 2022-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Toxins |
| spelling | doaj.art-f8c7904b69e44bd89b55f55789cdec7a2023-11-24T02:59:19ZengMDPI AGToxins2072-66512022-10-01141069710.3390/toxins14100697Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i>Rimma S. Kalina0Igor E. Kasheverov1Sergey G. Koshelev2Oksana V. Sintsova3Steve Peigneur4Ernesto Lopes Pinheiro-Junior5Roman S. Popov6Victoria E. Chausova7Margarita M. Monastyrnaya8Pavel S. Dmitrenok9Marina P. Isaeva10Jan Tytgat11Sergey A. Kozlov12Emma P. Kozlovskaya13Elena V. Leychenko14Irina N. Gladkikh15G.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, 117997 Moscow, RussiaShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, 117997 Moscow, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaToxicology and Pharmacology, Campus Gasthuisberg, University of Leuven (KU Leuven), 3000 Leuven, BelgiumToxicology and Pharmacology, Campus Gasthuisberg, University of Leuven (KU Leuven), 3000 Leuven, BelgiumG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaToxicology and Pharmacology, Campus Gasthuisberg, University of Leuven (KU Leuven), 3000 Leuven, BelgiumShemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Science, 117997 Moscow, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaG.B. Elyakov Pacific Institute of Bioorganic Chemistry, Far Eastern Branch, Russian Academy of Sciences, 690022 Vladivostok, RussiaThe nicotinic acetylcholine receptors (nAChRs) are prototypical ligand-gated ion channels, provide cholinergic signaling, and are modulated by various venom toxins and drugs in addition to neurotransmitters. Here, four APETx-like toxins, including two new toxins, named Hmg 1b-2 Met<sub>ox</sub> and Hmg 1b-5, were isolated from the sea anemone <i>Heteractis magnifica</i> and characterized as novel nAChR ligands and acid-sensing ion channel (ASIC) modulators. All peptides competed with radiolabeled α-bungarotoxin for binding to <i>Torpedo californica</i> muscle-type and human α7 nAChRs. Hmg 1b-2 potentiated acetylcholine-elicited current in human α7 receptors expressed in <i>Xenopus laevis</i> oocytes. Moreover, the multigene family coding APETx-like peptides library from <i>H. magnifica</i> was described and in silico surface electrostatic potentials of novel peptides were analyzed. To explain the 100% identity of some peptide isoforms between <i>H. magnifica</i> and <i>H. crispa</i>, 18S rRNA, COI, and ITS analysis were performed. It has been shown that the sea anemones previously identified by morphology as <i>H. crispa</i> belong to the species <i>H. magnifica</i>.https://www.mdpi.com/2072-6651/14/10/697sea anemonesphylogenyAPETx-like toxinsnicotinic acetylcholine receptorsacid-sensing ion channels |
| spellingShingle | Rimma S. Kalina Igor E. Kasheverov Sergey G. Koshelev Oksana V. Sintsova Steve Peigneur Ernesto Lopes Pinheiro-Junior Roman S. Popov Victoria E. Chausova Margarita M. Monastyrnaya Pavel S. Dmitrenok Marina P. Isaeva Jan Tytgat Sergey A. Kozlov Emma P. Kozlovskaya Elena V. Leychenko Irina N. Gladkikh Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i> Toxins sea anemones phylogeny APETx-like toxins nicotinic acetylcholine receptors acid-sensing ion channels |
| title | Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i> |
| title_full | Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i> |
| title_fullStr | Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i> |
| title_full_unstemmed | Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i> |
| title_short | Nicotinic Acetylcholine Receptors Are Novel Targets of APETx-like Toxins from the Sea Anemone <i>Heteractis magnifica</i> |
| title_sort | nicotinic acetylcholine receptors are novel targets of apetx like toxins from the sea anemone i heteractis magnifica i |
| topic | sea anemones phylogeny APETx-like toxins nicotinic acetylcholine receptors acid-sensing ion channels |
| url | https://www.mdpi.com/2072-6651/14/10/697 |
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