Binding of two P-III snake venom metalloproteinase (SVMPs), one procoagulant and one hemorrhagic, to microvessels was compared in an ex vivo model. The procoagulant SVMP did not bind to the microvasculature, in contrast to the clear localization on microvessels of the hemorrhagic SVMP. Deglycosylation of the procoagulant enzyme did not enable this toxin to bind to microvessels, suggesting that glycosylation is not interfering with binding. These observations suggest that procoagulant SVMPs lack exosites for interaction with microvessels components.
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http://dx.doi.org/10.1016/j.toxicon.2020.02.011 | DOI Listing |
Toxins (Basel)
November 2024
Laboratório de Matriz Extracelular e Biotecnologia de Venenos, Universidade Federal do Paraná, UFPR, Curitiba 81531-980, Brazil.
Heliyon
May 2024
State Key Laboratory of Functions and Applications of Medicinal Plants, Guizhou Medical University, Guiyang, 550014, China.
Snake venoms, comprising a complex array of protein-rich components, an important part of which are snake venom metalloproteinases (SVMPs). These SVMPs, which are predominantly isolated from viperid venoms, are integral to the pathology of snakebites. However, SVMPs derived from elapid venoms have not been extensively explored, and only a handful of SVMPs have been characterized to date.
View Article and Find Full Text PDFChem Biol Interact
May 2024
Laboratório de Imunologia Celular Aplicada à Saúde, Fundação Oswaldo Cruz, FIOCRUZ Rondônia, Porto Velho, RO, Brazil; Departamento de Medicina, Universidade Federal de Rondônia, UNIR, Porto Velho, RO, Brazil. Electronic address:
Snake venom metalloproteases (SVMPs) are hydrolytic enzymes dependent on metal binding, primarily zinc (Zn), at their catalytic site. They are classified into three classes (P-I to P-III). BjussuMP-II, a P-I SVMP isolated from Bothrops jararacussu snake venom, has a molecular mass of 24 kDa.
View Article and Find Full Text PDFJ Proteomics
March 2024
Clinical Toxicology Research Group, University of Newcastle N.S.W. 2308, Australia. Electronic address:
The Australian elapid snake radiation (Hydrophiinae) has evolved in the absence of competition from other advanced snakes. This has resulted in ecological specialisation in Australian elapids and the potential for venom proteomes divergent to other elapids. We characterised the venom of the Australian elapid Vermicella annulata (eastern bandy bandy).
View Article and Find Full Text PDFToxins (Basel)
September 2023
Department of Molecular Medicine, Faculty of Medicine, Universiti Malaya, Kuala Lumpur 50603, Malaysia.
The venom proteome of Temple Pit Viper () is unique among pit vipers, characterized by a high abundance of a neurotoxic peptide, waglerin. To further explore the genetic diversity of its toxins, the present study assembled the venom gland transcriptome of from west Malaysia. Among the 15 toxin gene families discovered, gene annotation and expression analysis reveal the dominating trend of bradykinin-potentiating peptide/angiotensin-converting enzyme inhibitor-C-type natriuretic peptide (BPP/ACEI-CNP, 76.
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