Venom complexity of Bothrops atrox (common lancehead) siblings

Abstract

Background: Variability in snake venoms is a well-studied phenomenon. However, sex-based variation of Bothrops atrox snake venom using siblings is poorly investigated. Bothrops atrox is responsible for the majority of snakebite accidents in the Brazilian Amazon region. Differences in the venom composition of Bothrops genus have been linked to several factors such as ontogeny, geographical distribution, prey preferences and sex. Thus, in the current study, venom samples of Bothrops atrox male and female siblings were analyzed in order to compare their biochemical and biological characteristics. Methods: Venoms were collected from five females and four males born from a snake captured from the wild in São Bento (Maranhão, Brazil), and kept in the Laboratory of Herpetology of Butantan Intitute. The venoms were analyzed individually and as a pool of each gender. The assays consisted in protein quantification, 1-DE, mass spectrometry, proteolytic, phospholipase A 2 , L-amino acid oxidase activities, minimum coagulant dose upon plasma, minimum hemorrhagic dose and lethal dose 50%. Results: Electrophoretic profiles of male's and female's venom pools were quite similar, with minor sex-based variation. Male venom showed higher LAAO, PLA 2 and hemorrhagic activities, while female venom showed higher coagulant activity. On the other hand, the proteolytic activities did not show statistical differences between pools, although some individual variations were observed. Meanwhile, proteomic profile revealed 112 different protein compounds; of which 105 were common proteins of female's and male's venom pools and seven were unique to females. Despite individual variations, lethality of both pools showed similar values. Conclusion: Although differences between female and male venoms were observed, our results show that individual variations are significant even between siblings, highlighting that biological activities of venoms and its composition are influenced by other factors beyond gender.

Bleeding and Thrombosis: Insights into Pathophysiology of Bothrops Venom-Related Hemostasis Disorders

“…Sex-based variation of B. atrox venom was observed even in siblings. Male venom showed higher LAAO, PLA 2 and hemorrhagic activities, while female venoms showed higher coagulant activity [103]. Venom from B. jararacussu males is more procoagulant than those of females [110].…”

From birth to adulthood: An analysis of the Brazilian lancehead (Bothrops moojeni) venom at different life stages

“…jararaca juveniles [ 96 ] and adults [ 42 ], in addition to adult B . atrox [ 37 ], although another work with newborn and adult B . jararaca did not present variation according to sex [ 36 ].…”

“…Considering how snake venom individual variability may affect the pool [ 34 , 37 ], we need to highlight that the Bm3 venoms used in this work had a particular characteristic: they were all from individuals of the same litter and male Bm3 was composed by only one individual. Collagenolytic activity, for example, as a proteolytic activity, is expected to be higher in older snakes [ 28 , 49 , 51 ] but Bm3 venoms showed an activity similar to BmN, Bm<1, and Bm1.…”

Two-Dimensional Blue Native/SDS Polyacrylamide Gel Electrophoresis for Analysis of Brazilian Bothrops Snake Venoms

“…In most Bothrops venoms, snake venom metalloproteinases (SVMPs) and snake venom serine proteinases (SVSPs) are the preponderant enzymes present therein [ 11 ]. Bothrops SVMPs are abundant enzymes, accounting for 42–72% of venom proteins in B. atrox [ 12 , 13 ], 10–37% in B. jararaca [ 14 , 15 ], and 39–49% in B. erythromelas [ 16 ]. They have been directly linked to the main effects observed during envenomation, such as blood incoagulability, hemorrhage, inflammation, and myonecrosis.…”

“…These enzymes are subdivided into groups according to their molecular mass and domain structure: P-I, P-II, and P-III [ 17 , 18 ]. SVSPs account for 4–11% of the venoms of B. atrox [ 12 , 13 ], 4–21% of B. erythromelas [ 16 ], and 13–29% of B. jararaca [ 14 , 15 ]. SVSPs have molecular masses of 26–67 kDa, and when isolated they show no toxic effects, but their biological interaction with other venom components causes hemostatic imbalance by interfering in the coagulation cascade, fibrinolysis, and platelet aggregation.…”