Purification and characterization of a metalloproteinase, Porthidin-1, from the venom of Lansberg’s hog-nosed pitvipers (Porthidium lansbergii hutmanni)
| Autor: | Elda E. Sánchez, W. Andy Tao, María E. Girón, Ana María Salazar, Belsy Guerrero, Amalid Estrella, Alexis Rodríguez-Acosta, Jacob A. Galan |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Male
Spectrometry Mass Electrospray Ionization Platelet Aggregation Molecular Sequence Data Poison control Venom Hemorrhage Biology Toxicology Article Microbiology Porthidium lansbergii Lethal Dose 50 Mice Viperidae Sequence Analysis Protein biology.animal Crotalid Venoms Animals Edema Humans Amino Acid Sequence Envenomation Metalloproteinase biology.organism_classification Molecular Weight Metalloproteases Bothrops Serine Proteinase Inhibitors |
| Popis: | Porthidium lansbergii hutmanni is a small pit viper found on Margarita Island, Venezuela. Local tissue damage is one of the most obvious characteristics of P. l. hutmanni envenomation, which can lead to diverse pathological effects, such as hemorrhage, edema, blistering, necrosis, lymphatic vessel damage and degradation of extracellular matrix. Metalloproteinases are one of the major components in venoms responsible for these effects. To date, very little is known or has been reported on P. l. hutmanni venom. Crude P. l. hutmanni venom had a LD(50) of 2.5 mg/kg and was considered very hemorrhagic (minimal hemorrhagic dose [MHD]: 0.98 μg) when compared to other hemorrhagic (Bothrops) venoms in Venezuela. Crude P. l. hutmanni venom also inhibited ADP-induced platelet aggregation. A metalloproteinase, Porthidin-1, from this venom was isolated by three chromatography steps (Sephadex G100, Superose 12 HR10/30 and Bioscale Q2). Porthidin-1 falls in the SVMP P-I class having a molecular weight of 23 kDa, verified by both SDS-PAGE and mass spectrometry. High-resolution mass spectrometry and a database search identified a peptide from Porthidin-1 (YNGDLDK) belonging to the SVMP family of proteins. Porthidin-1 contained hemorrhagic, fibrino(geno)lytic, caseinolytic and gelatinolytic activities, and these activities were capable of being neutralized by metalloproteinase inhibitors but not serine proteinase inhibitors. The peptide YNGDLDK shared similarities with five venom proteins with a BLAST e-value of |
| Databáze: | OpenAIRE |
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