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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

olecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish Thalassophryne maculos

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Author(s):
Lopes-Ferreira, Monica [1] ; Sosa-Rosales, Ines [2] ; Silva Junior, Pedro Ismael [3] ; Conceicao, Katia [4] ; Maleski, Adolfo Luis Almeida [1, 5] ; Balan-Lima, Leticia [1] ; Disner, Geonildo Rodrigo [1] ; Lima, Carla [1]
Total Authors: 8
Affiliation:
[1] Butantan Inst, Lab Appl Toxinol CeTICs FAPESP, Immunoregulat Unit, Vital Brasil Ave, 1500 Butantan, BR-05503009 Sao Paulo - Brazil
[2] Univ Oriente, Escuela Ciencias Aplicadas Mar, Boca Rio 6304 - Venezuela
[3] Butantan Inst, Lab Appl Toxinol CeTICs FAPESP, Prot Chem Unit, Vital Brasil Ave, 1500 Butantan, BR-05503009 Sao Paulo - Brazil
[4] UNIFESP, Peptide Biochem Lab, BR-12247014 Sao Jose Dos Campos - Brazil
[5] Butantan Inst, Postgrad Program Toxinol, Vital Brasil Ave, 1500 Butantan, BR-05503009 Sao Paulo - Brazil
Total Affiliations: 5
Document type: Journal article
Source: OXIN; v. 14, n. 1 JAN 2022.
Web of Science Citations: 1
Abstract

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 alpha 5 beta 1 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. (AU)

FAPESP's process: 13/07467-1 - CeTICS - Center of Toxins, Immune-Response and Cell Signaling
Grantee:Hugo Aguirre Armelin
Support Opportunities: Research Grants - Research, Innovation and Dissemination Centers - RIDC