Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Lopes-Ferreira, Monica, Sosa-Rosales, Ines, Silva Junior, Pedro Ismael, Conceicao, Katia, Maleski, Adolfo Luis Almeida, Balan-Lima, Leticia, Disner, Geonildo Rodrigo, Lima, Carla
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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
_version_ 1784637385924935680
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
work_keys_str_mv AT lopesferreiramonica molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT sosarosalesines molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT silvajuniorpedroismael molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT conceicaokatia molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT maleskiadolfoluisalmeida molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT balanlimaleticia molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT disnergeonildorodrigo molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa
AT limacarla molecularcharacterizationandfunctionalanalysisofthenattectinliketoxinfromthevenomousfishthalassophrynemaculosa