Individual Variability in the Venom Proteome of Juvenile Bothrops jararaca Specimens

Abstract

Snake venom proteomes/peptidomes are highly complex and subject to ontogenetic changes. Individual variation in the venom proteome of juvenile snakes is poorly known. We report the proteomic analysis of venoms from 21 juvenile specimens of Bothrops jararaca of different geographical origins and correlate it with the evaluation of important venom features. Individual venoms showed similar caseinolytic activities; however, their amidolytic activities were significantly different. Rather intriguingly, plasma coagulant activity showed remarkable variability among the venoms but not the prothrombin-activating activity. LC-MS analysis showed significant differences between venoms; however, an interesting finding was the ubiquitous presence of the tripeptide ZKW, an endogenous inhibitor of metalloproteinases. Electrophoretic profiles of proteins submitted to reduction showed significant variability in total proteins, glycoproteins, and in the subproteomes of proteinases. Moreover, identification of differential bands revealed variation in most B. jararaca toxin classes. Profiles of venoms analyzed under nonreducing conditions showed less individual variability and identification of proteins in a conserved band revealed the presence of metalloproteinases and l-amino acid oxidase as common components of these venoms. Taken together, our findings suggest that individual venom proteome variability in B. jararaca exists from a very early animal age and is not a result of ontogenetic and diet changes.

Intact protein mass spectrometry reveals intraspecies variations in venom composition of a local population of Vipera kaznakovi in Northeastern Turkey

“…The svSPs play a significant role in mammalian envenomation by affecting the hemostatic system through perturbing blood coagulation, typically via the inducement of fibrinogenolytic effects [79,80]. Taking this into account, a possible explanation could be that the lower svSP concentration observed in juveniles could be the result of differences in diet, as young animals typically prey on insects, before switching to feed upon small mammals and lizards as they become adults [81][82][83].…”

Multifunctional Toxins in Snake Venoms and Therapeutic Implications: From Pain to Hemorrhage and Necrosis

“…The dominant families are secreted phospholipases A 2 (PLA2s), snake venom metalloproteinases (SVMP), snake venom serine proteases (SVSP), and three-finger peptides (3FTX), while the secondary families comprise cysteine-rich secretory proteins, Lamino acid oxidases, kunitz peptides, C-type lectins, disintegrins, and natriuretic peptides (Slagboom et al, 2017;Tasoulis and Isbister, 2017;Munawar et al, 2018). Interestingly, snake venom composition varies interspecifically (Fry et al, 2008;Tasoulis and Isbister, 2017), as well as intraspecifically, with many factors influencing this diversity including age (Dias et al, 2013), gender (Menezes et al, 2006;Zelanis et al, 2016), location (Durban et al, 2011;Goncalves-Machado et al, 2016), diet (Barlow et al, 2009), and season (Gubensek et al, 1974). This variability phenomenon underpins toxin diversity and multifunctionality, and is of great importance to be considered in antivenom production and envenomation treatment .…”

Snake venoms are integrated systems, but abundant venom proteins evolve more rapidly

“…Consequently, although macroevolutionary patterns of individual venom proteins are somewhat understood, their regulation and microevolution remain almost entirely unknown [ 49 ]. However, if individual toxins (gene products) fluctuate in abundance and importance over short evolutionary time scales [ 50 ], evolutionary analysis of individual venom constituents may be misleading, as individual genes may experience different selective pressures from lineage to lineage. Furthermore, rates of venom protein evolution may depend on the relative abundance of various venom protein classes, and on their relative importance in immobilizing the prey.…”