Dolomedes mizhoanus and Dolomedes sulfurous are two venomous spiders found in the same area in southern China and are characterized by living in water plants and feeding on fish. In this study, the chemical compositions and activities of these venoms were compared. Both venoms contain hundreds of peptides as shown by off-line RP-HPLC/MALDI-TOF-MS analysis, but have a different peptide distribution, with D. mizhoanus venom containing fewer high molecular mass (7000-9000 Da) peptides (3%) than D. sulfurous venom (25.6%). Patch-clamp analyses showed that both venoms inhibited voltage-activated Na(+), K(+) and Ca(2+) channels in rat DRG neurons, however, differences in their inhibitory effects were observed. In general, D. mizhoanus venom had lower inhibitory activity than D. sulfurous venom and both venoms had a different inhibitory spectrum against these ion channels, showing that both venoms are useful for identifying antagonists to them. In addition, intrathoracic injection of both venoms caused severe neurotoxic effects in zebrafish and death at higher concentrations, respectively. Considering that both spiders belong to the same genus, live in the same area and have similar habits, elucidation of the differences between the peptide toxins from both venoms would provide new molecular insights into the evolution of spider peptides.
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http://dx.doi.org/10.1016/j.toxicon.2014.02.014 | DOI Listing |
Int J Biol Macromol
December 2024
Laboratory of Cellular Immunology Applied to Health, Oswaldo Cruz Foundation, FIOCRUZ Rondônia, Porto Velho, RO, Brazil; Department of Medicine, Federal University of Rondonia (UNIR), Porto Velho, RO, Brazil. Electronic address:
Phospholipases A (PLAs) are highly prevalent in Bothrops snake venom and play a crucial role in inflammatory responses and immune cell activation during envenomation. Despite their significance, the specific role of PLAs from Bothrops mattogrossensis venom (BmV) in inflammation is not fully understood. This study sought to isolate and characterize a novel acidic PLA from BmV, designated BmPLA-A, and to evaluate its effects on human umbilical vein endothelial cells (HUVECs), with a specific focus on cytotoxicity, adhesion, and detachment.
View Article and Find Full Text PDFSci Rep
December 2024
School of Biological Sciences, University of Utah, Salt Lake City, Utah, USA.
Voltage-gated potassium channels (VGKCs) comprise the largest and most complex families of ion channels. Approximately 70 genes encode VGKC alpha subunits, which assemble into functional tetrameric channel complexes. These subunits can also combine to form heteromeric channels, significantly expanding the potential diversity of VGKCs.
View Article and Find Full Text PDFVet Sci
November 2024
Department of Chemistry, Faculty of Veterinary Medicine, University of Belgrade, Bulevar Oslobođenja 18, 11000 Belgrade, Serbia.
Deep proteomic analyses identified, in total, 159 master proteins (with 1% FDR and 2 unique peptides) from 26 protein families in the venom of Data are available via ProteomeXchange with the identifier PXD056495. The relative abundance of PLA2s is 11.60% of the crude venom, of which 4.
View Article and Find Full Text PDFTrop Med Infect Dis
December 2024
Institut Pasteur Medical Center, Paris Cité University, F-75015 Paris, France.
Snakes responsible for bites are rarely identified, resulting in a loss of information about snakebites from venomous species whose venom effects are poorly understood. A prospective clinical study including patients bitten by a snake was conducted in Cameroon between 2019 and 2021 to evaluate the efficacy and tolerability of a marketed polyvalent antivenom. Clinical presentation during the first 3 days of hospitalization was recorded following a standardized protocol.
View Article and Find Full Text PDFToxins (Basel)
December 2024
National Natural Toxins Research Center (NNTRC), Texas A&M University-Kingsville, Kingsville, TX 78363, USA.
King cobra () venom comprises a diverse array of proteins and peptides. However, the roles and properties of these individual components are still not fully understood. Among these, Cysteine-rich secretory proteins (CRiSPs) are recognized but not fully characterized.
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