Molecular Characterization and Functional Analysis of the Nattectin-like Toxin from the Venomous Fish .

Toxins (Basel)

Immunoregulation Unit of the Laboratory of Applied Toxinology (CeTICs/FAPESP), Butantan Institute, Vital Brasil Avenue, 1500 Butantan, Sao Paulo 05503-009, Brazil.

Published: December 2021

TmC4-47.2 is a toxin with myotoxic activity found in the venom of , 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 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 , pointing to its role as a molecule involved in the carbohydrate-independent agglutination response and modulation of eosinophilic and neutrophilic inflammation.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8778695PMC
http://dx.doi.org/10.3390/toxins14010002DOI Listing

Publication Analysis

Top Keywords

venomous fish
8
molecular characterization
4
characterization functional
4
functional analysis
4
analysis nattectin-like
4
nattectin-like toxin
4
toxin venomous
4
tmc4-472
4
fish tmc4-472
4
tmc4-472 toxin
4

Similar Publications

Background: Animal venom systems are considered as valuable model for investigating the molecular mechanisms underlying phenotypic evolution. Stonefish are the most venomous and dangerous fish because of severe human envenomation and occasionally fatalities, whereas the genomic background of their venom has not been fully explored compared with that in other venomous animals.

Results: In this study, we followed modern venomic pipelines to decode the Synanceia verrucosa venom components.

View Article and Find Full Text PDF

Aim: This study aimed to create an f9l mutant zebrafish using clustered regularly interspaced short palindromic repeats (CRISPR)/CRISPR-associated protein 9 (Cas9) and characterize its coagulation properties to investigate its functional similarity to human FX and explore the potential synergy between f9l and f10.

Methods: Three gRNAs targeting exon 8 encoded by the catalytic domain of the f9l gene were injected into 300 single-cell zebrafish embryos using CRISPR/Cas9 technology. DNA from the resulting adults was extracted from tail tips, and PCR was used to detect indels.

View Article and Find Full Text PDF

Yessotoxin is one of the shellfish toxins leading to mussel farm closures in the Adriatic Sea of Italy. Two putative Gonyaulax spinifera strains GSA0501 and GSA0602 are known as yessotoxins producers, but their identities have remained elusive since 2005. To address this gap, we established five Gonyaulax strains by incubating sediments from the Adriatic Sea and subsequently isolating single cells.

View Article and Find Full Text PDF

Saxitoxin (STX) is a potent neurotoxin naturally produced by dinoflagellates and cyanobacteria. STX inhibits voltage-gated sodium channels (VGSCs), affecting the propagation of action potentials. Consumption of seafood contaminated with STX is responsible for paralytic shellfish poisoning (PSP).

View Article and Find Full Text PDF
Article Synopsis
  • The stonefish species Synanceia verrucosa and Synanceia horrida are among the most venomous fish, known for causing severe stings in humans, prompting research into their venom components.
  • This study shifted focus from proteins to small molecules in stonefish venom and identified three new substances: γ-aminobutyric acid (GABA), choline, and 0-acetylcholine, with GABA being the first of its kind found in fish venom.
  • The research revealed how these venoms activate specific human receptors and demonstrated distinct cytotoxic effects, suggesting a need for further exploration of these small molecules to improve understanding and treatment of sting-related symptoms.
View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!