Elsevier

Toxicon

Volume 96, 15 March 2015, Pages 46-49
Toxicon

Short communication
Neuromuscular effects of venoms and crotoxin-like proteins from Crotalus durissus ruruima and Crotalus durissus cumanensis

https://doi.org/10.1016/j.toxicon.2015.01.006Get rights and content

Highlights

  • Neurotoxicity and myotoxicity of Viperidae venoms were compared in vitro.

  • Crotalus durissus ruruima venom presented only neurotoxic activity.

  • Crotalus durissus cumanensis venom presented neurotoxic and myotoxic activities.

  • C. durissus cumanensis venom is more potent than C. durissus ruruima.

  • Crotoxins found in both venoms were the main cause of their neurotoxicity.

Abstract

A myographic study was performed to compare the neuromuscular effects of venoms and crotoxin-like proteins from Crotalus durissus ruruima and Crotalus durissus cumanensis in mice phrenic-diaphragm preparation. It was concluded that both venoms present neurotoxic activity as a consequence of their crotoxin content. Furthermore, crotoxin from C.d. cumanensis is more potent than that from C.d. ruruima venom. At the concentration range in which both venoms express neurotoxic activity, only C.d. cumanensis venom also manifest a direct myotoxic effect that probably involves the synergic participation of other components than crotoxin.

Section snippets

Ethical standards

Animal handling and experiments were in accordance with the National Research Council (NRC) Guide and the necessary permission has been obtained from the local ethics committee (058/06-CEEA).

References (34)

  • J.A. Pereañez et al.

    Biochemical and biological characterization of a PLA2 from crotoxin complex of Crotalus durissus cumanensis

    Toxicon

    (2009)
  • L.A. Ponce-Soto et al.

    Structural and pharmacological characterization of the crotamine isoforms III-4 (MYX4_CROCu) and III-7 (MYX7_CROCu) isolated from the Crotalus durissus cumanensis venom

    Toxicon

    (2010)
  • F.F. Romero-Vargas et al.

    Biological and biochemical characterization of two new PLA2 isoforms Cdc-9 and Cdc-10 from Crotalus durissus cumanensis snake venom

    Comp. Biochem. Physiol. C Toxicol. Pharmacol.

    (2010)
  • T.F. Salvini et al.

    Systemic skeletal muscle necrosis induced by crotoxin

    Toxicon

    (2001)
  • D.G. Beghini et al.

    Enzymatic characterization of a novel phospholipase A2 from Crotalus durissus cascavella rattlesnake (Maracambóia) venom

    J. Protein Chem.

    (2000)
  • C. Bon et al.

    Crotoxin, half-century of investigations on a phospholipase A2 neurotoxin

    Acta Physiol. Pharmacol. Latinoam.

    (1989)
  • C. Bon et al.

    Postsynaptic effects of crotoxin and of its isolated subunits

    Eur. J. Biochem.

    (1979)
  • Cited by (16)

    • Biological and proteomic characterization of the venom from Peruvian Andes rattlesnake Crotalus durissus

      2022, Toxicon
      Citation Excerpt :

      These toxins concentration vary among Crotalic venoms. It has been documented in C. durissus venom proteomic studies that crotoxin accounts for 70–90% (Francischetti et al., 2000; Saravia et al., 2002; Luís et al., 2015; Calvete et al., 2010a; Boldrini-frança et al., 2010) and crotamine constitutes from 2 to 22% of the found protein venom content (Calvete et al., 2010a; Schenberg, 1959; Oguiura et al., 2009; Lourenço et al., 2013). Snake venom composition can be influenced by several factors including geographical origin, feeding habits, sex and age of the snake, generating inter and intraspecific variations (Barlow et al., 2009; Chippaux et al., 1991).

    • Revisiting the potential of South American rattlesnake Crotalus durissus terrificus toxins as therapeutic, theranostic and/or biotechnological agents

      2022, Toxicon
      Citation Excerpt :

      The venom of Crotalus snakes contains enzymes that are responsible for the main symptoms of the envenomation by these rattlesnakes, and many of these deleterious effects have been linked to the actions of metallo- and serine-protease, such as crotoxin, but the participation of other proteolytic enzymes with hemostatic properties, including phosphodiesterases, hyaluronidases, L-amino acid oxidases (LAAOs), and non-enzyme neurotoxins, such as crotamine, among other toxins, are also recognized (Hernández et al., 2007; Suntravat et al., 2013). For instance, the South American C. d. vegrandis venom is neurotoxic and contains several isomers of crotoxin (Kaiser and Aird 1987; Aird et al., 1989), while the venom of the South American C. d. cumanensis is composed by crotamine, gyroxin, convulxin and crotoxin, among other toxins, and is also commonly recognized as neurotoxic (Aguilar et al., 2007; Cavalcante et al., 2015). In general, these toxins have also been associated with local tissue damage and necrosis, although they are observed mainly in the envenomation by the North American Crotalus snakes, while in South America, these localized effects are more limited to very few snakes only (Sánchez and Rodríguez-Acosta, 2016).

    • Varespladib (LY315920) prevents neuromuscular blockage and myotoxicity induced by crotoxin on mouse neuromuscular preparations

      2021, Toxicon
      Citation Excerpt :

      The CTX neurotoxicity results from the summation of a remarkable presynaptic action, which reduces the acetylcholine release from motor nerve terminals (Brazil and Excell, 1971; Chang and Lee, 1977; Hawgood and Smith, 1977; Hawgood and Santana de Sá, 1979; Cavalcante et al., 2017; Bickler, 2020), with a minor postsynaptic action that causes desensitization of the nicotinic receptor (Vital Brazil, 1966; Bon et al., 1979). Moreover, the myotoxicity of CTX is not the preponderant effect, but it is related to the damage of muscle fibers, and it could contribute to paralysis (Hawgood and Smith, 1977; Gopalakrishnakone and Hawgood, 1984; Mebs and Ownby, 1990; Oshima-Franco et al., 1999; Melo et al., 2004; Cavalcante et al., 2015). The low toxicity of CB is related to the absence of CA, a subunit that acts as a chaperone preventing the binding of CB to non-specific sites (Habermann and Breithaupt, 1978; Jeng et al., 1978; Bon et al., 1979; Délot and Bon, 1993), requiring higher concentrations to produce CTX similar effects (Hawgood and Santana de Sá, 1979; Cavalcante et al., 2017).

    • Envenoming by the rattlesnake Crotalus durissus ruruima in the state of roraima, Brazil

      2020, Toxicon: X
      Citation Excerpt :

      The caseinolytic activity of the yellow venom of C. d. ruruima is three-fold higher than the white venom of C. d. terrificus or C. d. ruruima. On the other hand, Cavalcante and Ponce-Soto (2015) showed that the venom of C. d. ruruima and C. d. . cumanensis displays neurotoxic activity due to crotoxin activity, and crotoxin from C. d. cumanensis was more potent than that from C. d. ruruima venom.

    View all citing articles on Scopus
    View full text