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Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa
TmC4-47.2 is a toxin with myotoxic activity found in the venom of Thalassophryne maculosa, a venomous fish commonly found in Latin America whose envenomation produces an injury characterized by delayed neutrophil migration, production of major pro-inflammatory cytokines, and necrosis at the wound si...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778695/ https://www.ncbi.nlm.nih.gov/pubmed/35050979 http://dx.doi.org/10.3390/toxins14010002 |
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author | Lopes-Ferreira, Monica Sosa-Rosales, Ines Silva Junior, Pedro Ismael Conceicao, Katia Maleski, Adolfo Luis Almeida Balan-Lima, Leticia Disner, Geonildo Rodrigo Lima, Carla |
author_facet | Lopes-Ferreira, Monica Sosa-Rosales, Ines Silva Junior, Pedro Ismael Conceicao, Katia Maleski, Adolfo Luis Almeida Balan-Lima, Leticia Disner, Geonildo Rodrigo Lima, Carla |
author_sort | Lopes-Ferreira, Monica |
collection | PubMed |
description | TmC4-47.2 is a toxin with myotoxic activity found in the venom of Thalassophryne maculosa, a venomous fish commonly found in Latin America whose envenomation produces an injury characterized by delayed neutrophil migration, production of major pro-inflammatory cytokines, and necrosis at the wound site, as well as a specific systemic immune response. However, there are few studies on the protein structure and functions associated with it. Here, the toxin was identified from the crude venom by chromatography and protein purification systems. TmC4-47.2 shows high homology with the Nattectin from Thalassophryne nattereri venom, with 6 cysteines and QPD domain for binding to galactose. We confirm its hemagglutinating and microbicide abilities independent of carbohydrate binding, supporting its classification as a nattectin-like lectin. After performing the characterization of TmC4-47.2, we verified its ability to induce an increase in the rolling and adherence of leukocytes in cremaster post-capillary venules dependent on the α5β1 integrin. Finally, we could observe the inflammatory activity of TmC4-47.2 through the production of IL-6 and eotaxin in the peritoneal cavity with sustained recruitment of eosinophils and neutrophils up to 24 h. Together, our study characterized a nattectin-like protein from T. maculosa, pointing to its role as a molecule involved in the carbohydrate-independent agglutination response and modulation of eosinophilic and neutrophilic inflammation. |
format | Online Article Text |
id | pubmed-8778695 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-87786952022-01-22 Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa Lopes-Ferreira, Monica Sosa-Rosales, Ines Silva Junior, Pedro Ismael Conceicao, Katia Maleski, Adolfo Luis Almeida Balan-Lima, Leticia Disner, Geonildo Rodrigo Lima, Carla Toxins (Basel) Article TmC4-47.2 is a toxin with myotoxic activity found in the venom of Thalassophryne maculosa, a venomous fish commonly found in Latin America whose envenomation produces an injury characterized by delayed neutrophil migration, production of major pro-inflammatory cytokines, and necrosis at the wound site, as well as a specific systemic immune response. However, there are few studies on the protein structure and functions associated with it. Here, the toxin was identified from the crude venom by chromatography and protein purification systems. TmC4-47.2 shows high homology with the Nattectin from Thalassophryne nattereri venom, with 6 cysteines and QPD domain for binding to galactose. We confirm its hemagglutinating and microbicide abilities independent of carbohydrate binding, supporting its classification as a nattectin-like lectin. After performing the characterization of TmC4-47.2, we verified its ability to induce an increase in the rolling and adherence of leukocytes in cremaster post-capillary venules dependent on the α5β1 integrin. Finally, we could observe the inflammatory activity of TmC4-47.2 through the production of IL-6 and eotaxin in the peritoneal cavity with sustained recruitment of eosinophils and neutrophils up to 24 h. Together, our study characterized a nattectin-like protein from T. maculosa, pointing to its role as a molecule involved in the carbohydrate-independent agglutination response and modulation of eosinophilic and neutrophilic inflammation. MDPI 2021-12-21 /pmc/articles/PMC8778695/ /pubmed/35050979 http://dx.doi.org/10.3390/toxins14010002 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Lopes-Ferreira, Monica Sosa-Rosales, Ines Silva Junior, Pedro Ismael Conceicao, Katia Maleski, Adolfo Luis Almeida Balan-Lima, Leticia Disner, Geonildo Rodrigo Lima, Carla Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa |
title | Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa |
title_full | Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa |
title_fullStr | Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa |
title_full_unstemmed | Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa |
title_short | Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculosa |
title_sort | molecular characterization and functional analysis of the nattectin-like toxin from the venomous fish thalassophryne maculosa |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778695/ https://www.ncbi.nlm.nih.gov/pubmed/35050979 http://dx.doi.org/10.3390/toxins14010002 |
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