ABSTRACT
Snake venoms are a complex mixture of components, which have a wide range of actions both on prey and human victims. The genus Bothrops causes the vast majority of snakebites in Central and South America, being responsible for 80% of snake envenomations in Brazil. Envenomations are characterizedby prominent local effects, including oedema, haemorrhage and necrosis, which can lead to permanent disability. Systemic manifestations such as haemorrhage, coagulopathy, shock and acute renal failure may also occur.In the present study we have investigated the action of venoms from 19 species of snakes from the genus Bothrops, occurring in Brazil, on the complement system in in vitro studies. All venoms were able to activate the classical complement pathway, in the absence of sensitizing antibody. This activation wasin part associated with the cleavage of C1-Inhibitor by proteases present in these venoms, which disrupts complement activation control. No modification of the membrane bound complement regulators, such as DAF, CR1 and CD59 was detected, after treatment of human erythrocytes with the snake venoms. Some of the Bothrops venoms were also able to activate alternative and lectin pathways, as measured in haemolytic and ELISA assays. C3a, C4a and C5a were generated in sera treated with the venoms, not only through C-activation, but also by the direct cleavage of complement components, as determined using purified C3 and C4. Metallo- and/or serine-protease inhibitors prevented cleavage of C3 and C4. Theseresults suggest that Bothrops venoms can activate the complement system, generating a large amount of anaphylatoxins, which may play an important role in the inflammatory process presented in humans after snake envenomations, and they may also assist, due to their vasodilatory effects, to enhance the spreading of other venom components.
Subject(s)
Humans , Animals , Bothrops , Snakes/classification , Snake Venoms , Snake Venoms/antagonists & inhibitors , Snake Venoms/adverse effects , Snake Venoms/toxicity , Central America , South America , BrazilABSTRACT
Ctenus medius Keyserling, 1891 (Araneae: Ctenidae) co-occurs in various microhabitats of the Brazilian Atlantic Forest and can be easily misidentified as the medically important spider Phoneutria nigriventer Keyserling, 1981 (Ctenidae). Despite being phylogenetically close to Phoneutria, no data are available about the toxic potential of Ctenus medius venom. Here we show that, although presenting different profile of protein composition, C. medius venom displays some of the toxic properties exhibited by P. nigriventer venom, including proteolytic, hyaluronidasic and phospholipasic activities, as well as the ability of causing hyperalgesia and edema. Moreover, C. medius venom interferes in the activation of the complement system in concentrations that P. nigriventer venom is inactive. Thus, these data show that venoms of spiders from Ctenidae family share important proinflammatory properties and suggest that the C. medius bite may have an important noxious effect in human accidents.
Subject(s)
Spider Venoms/toxicity , Spiders/chemistry , Animals , Blotting, Western , Edema/chemically induced , Electrophoresis, Polyacrylamide Gel , Female , Hyperalgesia/chemically induced , Male , Rats , Rats, Wistar , Spider Venoms/enzymologyABSTRACT
Ctenus medius Keyserling, 1891 (Araneae: Ctenidae) co-occurs in various microhabitats of the Brazilian Atlantic Forest and can be easily misidentified as the medically important spider Phoneutria nigriventer Keyserling, 1981 (Ctenidae). Despite being phylogenetically close to Phoneutria, no data are available about the toxic potential of Ctenus medius venom. Here we show that, although presenting different profile of protein composition, C. medius venom displays some of the toxic properties exhibited by P. nigriventer venom, including proteolytic, hyaluronidasic and phospholipasic activities, as well as the ability of causing hyperalgesia and edema. Moreover, C. medius venom interferes in the activation of the complement system in concentrations that P. nigriventer venom is inactive. Thus, these data show that venoms of spiders from Ctenidae family share important proinflammatory properties and suggest that the C. medius bite may have an important noxious effect in human accidents.
Subject(s)
Male , Female , Humans , Child , Adolescent , Adult , Aged , Spider Venoms/poisoning , Spider Venoms/toxicityABSTRACT
The genus Bothrops spp. is responsible for 90% of envenomation by snakes in Brazil, and the standard treatment for snakebites is the antivenom therapy. The anti-bothropic serum produced by Butantan Institute is prepared by the hyperimmunization of horses with a pool of venoms from Bothrops alternatus, Bothrops jararaca, Bothrops jararacussu, Bothrops moojeni and Bothrops neuwiedi. In this study, the biochemical and biological characteristics of the venoms from nineteen snakes of the genus Bothrops, responsible for human accidents in Brazil, were analysed. Venoms, particularly from Crotalidae and Viperidae snakes, are rich sources of serine proteases and metalloproteases and the ability of the Brazilian anti-bothropic serum to neutralize the proteolytic activity of these venoms were also tested. The results obtained here show the existence of a large range of variation in the composition and activities in Bothrops spp. toxins and demonstrate that the anti-bothropic serum is not able to fully neutralize the toxic activities of all analysed venoms. These suggest that for the preparation of a fully effective therapeutic anti-bothropic serum, other venoms should be included in the immunization mixture.
Subject(s)
Bothrops , Crotalid Venoms/chemistry , Crotalid Venoms/toxicity , Animals , Antivenins/immunology , Brazil , Cross Reactions , Crotalid Venoms/classification , Crotalid Venoms/immunology , Horses , Hyaluronoglucosaminidase/metabolism , Lethal Dose 50 , Male , Mice , Neutralization Tests , Peptide Hydrolases/metabolism , Phospholipases A2/metabolism , Species SpecificityABSTRACT
The genus Bothrops spp. is responsible for 90% of envenomation by snakes in Brazil, andthe standard treatment for snakebites is the antivenom therapy. The anti-bothropic serumproduced by Butantan Institute is prepared by the hyperimmunization of horses witha pool of venoms from Bothrops alternatus, Bothrops jararaca, Bothrops jararacussu, Bothropsmoojeni and Bothrops neuwiedi. In this study, the biochemical and biological characteristicsof the venoms from nineteen snakes of the genus Bothrops, responsible for human accidentsin Brazil, were analysed. Venoms, particularly from Crotalidae and Viperidae snakes,are rich sources of serine proteases and metalloproteases and the ability of the Braziliananti-bothropic serum to neutralize the proteolytic activity of these venoms were alsotested. The results obtained here show the existence of a large range of variation in thecomposition and activities in Bothrops spp. toxins and demonstrate that the anti-bothropicserum is not able to fully neutralize the toxic activities of all analysed venoms. Thesesuggest that for the preparation of a fully effective therapeutic anti-bothropic serum, othervenoms should be included in the immunization mixture.
