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group_3_presentation_3_-_snake_venom [2017/12/01 23:46] rajendaa [History] |
group_3_presentation_3_-_snake_venom [2018/01/25 15:18] (current) |
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| - | ====== Evolution of Venom ====== | + | ====== Evolution of Snake Venom ====== |
| There is an evolutionary relationship within the clade containing snakes, anguimorphs, iguanians, and amphisbaenians, lacertids and teiioids (Fry et al., 2012). In particular, within the clade of Toxicofera, which contains snakes, anguimorphs, and iguanians it has been demonstrated that the evolution of venom has diversified the species within this clade. In fact, 170 million years ago, there was an actual point at which venom within all these species diversified (Fry et al., 2012). | There is an evolutionary relationship within the clade containing snakes, anguimorphs, iguanians, and amphisbaenians, lacertids and teiioids (Fry et al., 2012). In particular, within the clade of Toxicofera, which contains snakes, anguimorphs, and iguanians it has been demonstrated that the evolution of venom has diversified the species within this clade. In fact, 170 million years ago, there was an actual point at which venom within all these species diversified (Fry et al., 2012). | ||
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| - | **Figure 11: Timeline of Snake Venom Metalloproteinases (SVMPs) Research.** | + | **Figure 11: Timeline of Snake Venom Metalloproteinases (SVMPs) Research** |
| In particular, there has been, “significant progress…regarding the function, structure and role of the snake venom metalloproteinases (SVMPs) in viperid venom pathogenesis” (Fox and Serrano, 2009). As seen in Figure 11, since 1881 to the time of Fox and Serrano’s review paper in 2007, there have been several notable discoveries (Fox and Serrano, 2009). To begin with, in 1881 it was proposed that venoms could be proteolytic and in 1990 when it was seen that venom could coagulate blood, the proteolytic enzyme activity of venom was hinted at. Then around 1960, toxins extracted from snake venom were discovered to be proteinases and were shown to have a high metal content. Thus researchers came to know of snake venom metalloproteinases. Then over the next half century numerous SVMPs have been identified and their various roles and functions have been speculated upon. One of the key discoveries made was the connection between SVMPs and the ADAMs group of proteins. This led to the creation of the protein group: reprolysins. Current research, around 2007, focused on the evolutionary basis for SVMPs and future studies may focus on elucidating a better understanding of the structure and function of different SVMP types (Fox and Serrano, 2009). | In particular, there has been, “significant progress…regarding the function, structure and role of the snake venom metalloproteinases (SVMPs) in viperid venom pathogenesis” (Fox and Serrano, 2009). As seen in Figure 11, since 1881 to the time of Fox and Serrano’s review paper in 2007, there have been several notable discoveries (Fox and Serrano, 2009). To begin with, in 1881 it was proposed that venoms could be proteolytic and in 1990 when it was seen that venom could coagulate blood, the proteolytic enzyme activity of venom was hinted at. Then around 1960, toxins extracted from snake venom were discovered to be proteinases and were shown to have a high metal content. Thus researchers came to know of snake venom metalloproteinases. Then over the next half century numerous SVMPs have been identified and their various roles and functions have been speculated upon. One of the key discoveries made was the connection between SVMPs and the ADAMs group of proteins. This led to the creation of the protein group: reprolysins. Current research, around 2007, focused on the evolutionary basis for SVMPs and future studies may focus on elucidating a better understanding of the structure and function of different SVMP types (Fox and Serrano, 2009). | ||
