The Inhibiting Effect of Snake Bloods Upon the Hemorrhagic Action of Viper Venoms on Mice

Rosenfeld, Samuel S.; Glass, Sanford

doi:10.1097/00000441-194004000-00005

Cited by 17 publications

(3 citation statements)

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“…EIS occupy a similar ecological niche as snakes of the genus Lampropeltis (kingsnakes) that also possess serum-based inhibition of pitviper venom (Rosenfeld and Glass, 1940; Bonnett and Guttman, 1971; Philpot et al, 1978; Weinstein et al, 1992). Both kingsnakes and EIS are ophiophagous and exhibit a preference for pitviper prey (Weldon and Schell, 1984; Goetz et al, 2018) but are not considered dietary specialists.…”

Section: Discussionmentioning

confidence: 99%

Serum-based inhibition of pitviper Venom by Eastern Indigo Snakes (Drymarchon couperi)

et al. 2019

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When organisms possess chemical defenses, their predators may eventually evolve resistance to their toxins. Eastern indigo snakes ( Drymarchon couperi ; EIS) prey on pitvipers and are suspected to possess physiological resistance to their venom. In this study, we formally investigated this hypothesis using microassays that measured the ability of EIS blood sera to inhibit (A) hemolytic and (B) snake venom metalloproteinase (SVMP) activity of copperhead ( Agkistrodon contortrix ) venom. To serve as controls, we also tested the inhibitory ability of sera from house mice ( Mus musculus ) and checkered gartersnakes ( Thamnophis marcianus ), a snake that does not feed on pitvipers. Sera from both EIS and gartersnakes inhibited over 60% of SVMP activity, while only EIS sera also inhibited venom hemolytic activity (78%). Our results demonstrate that EIS serum is indeed capable of inhibiting two of the primary classes of toxins found in copperhead venom, providing the first empirical evidence suggesting that EIS possess physiological resistance to venom upon injection. Because we documented resistance to hemolytic components of pitviper venom within EIS but not gartersnakes, we speculate this resistance may be driven by selection from feeding on pitvipers while resistance to SVMP may be relatively widespread among snakes.

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Section: Discussionmentioning

confidence: 99%

Serum-based inhibition of pitviper Venom by Eastern Indigo Snakes (Drymarchon couperi)

et al. 2019

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“…A number of venomous and nonvenomous snake species are naturally resistant to the deleterious actions of snake venom components, in many cases due to the presence of specific antitoxins in their circulating blood [1–10]. These antitoxins were identified as liver-secreted proteins, which prevent any possible damage from toxins that might have reached the snake’s blood stream [11].…”

Section: Introductionmentioning

confidence: 99%

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Campos-Júnior

Melo

Dias

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 inhibitors, which primarily neutralize toxic phospholipases A2 that may eventually reach their circulation. This inhibitor type is generally known as snake blood phospholipase A2 inhibitors (sbPLIs). Most, if not all sbPLIs are oligomeric glycosylated proteins, although the carbohydrate moiety may not be essential for PLA2 inhibition in every case. The presently known sbPLIs belong to one of three structural classes – namely sbαPLI, sbβPLI or sbγPLI – depending on the presence of characteristic C-type lectin-like domains, leucine-rich repeats or three-finger motifs, respectively. Currently, the most numerous inhibitors described in the literature are sbαPLIs and sbγPLIs, whereas sbβPLIs are rare. When the target PLA2 is a Lys49 homolog or an Asp49 myotoxin, the sbPLI is denominated a myotoxin inhibitor protein (MIP). In this brief overview, the most relevant data on sbPLIs will be presented. Representative examples of sbαPLIs and sbγPLIs from two Old World – Gloydius brevicaudus and Malayopython reticulatus – and two New World – Bothrops alternatus and Crotalus durissus terrificus – snake species will be emphasized.

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“…Whereas most serum antitoxins of venomous snakes have been discovered by the observation of their protective effect [2][3][4][5][6][7][8][9][10], CSAP probably was the first to be discovered by electrophoresis. When a mixture of the serum and the venom of the cobra was subjected to electrophoresis, a new band was found which migrated behind that of serum albumin towards the positive electrode.…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization and binding interactions of the Chinese-cobra (Naja naja atra) serum antitoxic protein CSAP

Shao¹,

Shen²,

Havsteen

1993

Biochemical Journal

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The characterization of the single-chain protein in Chinese-cobra (Naja naja atra) blood serum, which yields strong specific protection against the venom of the same snake, is reported. The protein, CSAP (cobra serum antitoxic protein), was purified to electrophoretic homogeneity. Over the pH range 5-9 it formed stable complexes with the neuro- and the cardio-toxin of the snake. The molecular size of the CSAP was estimated to be 70.3 +/- 0.3 kDa. Tryptic hydrolysis of CSAP yielded several peptides that were able to bind to the toxin. The native CSAP maximally bound 8 +/- 1 toxin molecules/molecule. Six tryptic fragments, containing 5-39 residues, were sequenced. The longest of these displayed sequence similarity to rat serum albumin. The protective effect of the CSAP was demonstrated in vivo on mice and in vitro by measurement of the rate of haemolysis. Kinetic and thermodynamic parameters of the binding interactions of the neurotoxin and the CSAP were determined from the rates of displacement of 125I-labelled toxin from its complexes with the CSAP by unlabelled toxin by using a DEAE-cellulose filter assay for CSAP-toxin complexes. The toxin molecules rapidly dissociated from one type of site and slowly from a second. The binding capacity and concentration of the CSAP suffice to explain the protective effect of the latter against the toxin.

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The Inhibiting Effect of Snake Bloods Upon the Hemorrhagic Action of Viper Venoms on Mice

Cited by 17 publications

References 0 publications

Serum-based inhibition of pitviper Venom by Eastern Indigo Snakes (Drymarchon couperi)

Serum-based inhibition of pitviper Venom by Eastern Indigo Snakes (Drymarchon couperi)

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Purification, characterization and binding interactions of the Chinese-cobra (Naja naja atra) serum antitoxic protein CSAP

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