Proteomic profiling of snake venom metalloproteinases (SVMPs): insights into venom induced pathology.
Bothrops sp. snakebites account for the majority of envenomations in South and Central America. Bothrops jararaca accidents are characterized by edema, hemorrhage and necrosis, mainly attributed to the action of hemorrhagic snake venom metalloproteinases (SVMPs). Interestingly, accidents involving Bothrops lanceolatus (Fer-de-Lance) have a prothrombotic profile with necrosis and hemorrhage rarely reported. Here we describe biochemical and proteomic approaches to compare the venom composition of these snakes, focusing on the presence and activity of SVMPs. The total relative amount of SVMPs was found to be approximately the same in the venom of both species, the difference being in the distribution of SVMPs subgroups. Fer-de-Lance venom has relatively more PI SVMPs peptides identified (23-16%) while Jararaca venom has a higher amount of PIII SVMPs (54-43%). Gelatinolytic activity in the PIII mass range is also higher in Jararaca venom. Interestingly, the homologous band region in the Fer-de-Lance zymogram was only very weakly gelatinolytic. According to these findings it is feasible that the different distribution of SVMPs subgroups and their particular biochemical and pharmacological characteristics are two of the main factors contributing to these two radically different venom induced pathologies.
Terra
Renata M S
RM
Department of Microbiology, Health Sciences Center, University of Virginia, Charlottesville, VA, USA.
Pinto
Antônio F M
AF
Guimarães
Jorge A
JA
Fox
Jay W
JW
D000818:Animals; D017837:Bothrops; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D045726:Metalloproteases / Q000378:metabolism*; D020543:Proteome; D012910:Snake Venoms / Q000201:enzymology* / Q000633:toxicity; D053719:Tandem Mass Spectrometry
D020543:Proteome; D012910:Snake Venoms; D045726:Metalloproteases