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.
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http://dx.doi.org/10.3390/toxins14010002 | DOI Listing |
BMC Genomics
December 2024
Center for Evolution and Conservation Biology, Southern Marine Science and Engineering Guangdong Laboratory (Guangzhou), Guangzhou, China.
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.
Blood Coagul Fibrinolysis
December 2024
Department of Biological Sciences, University of North Texas, Denton, Texas, USA.
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.
Harmful Algae
January 2025
Third Institute of Oceanography, Ministry of Natural Resources, Xiamen 361005, China. Electronic address:
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 PDFNeurotoxicology
December 2024
Biology Department and Center for Oceans and Human Health,Woods Hole Oceanographic Institution, Woods Hole, Massachusetts 02543, USA.
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 PDFFEBS Open Bio
November 2024
Australian Institute of Tropical Health and Medicine, James Cook University, Cairns, Australia.
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