Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment
The venom of the snake Bothrops asper, the most important poisonous snake in Central America, evokes an inflammatory response, the mechanisms of which are not well characterized. The objectives of this study were to investigate whether B. asper venom and its purified toxins – phospholipases and met...
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| Format: | Article |
| Language: | English |
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Wiley
2000-01-01
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| Series: | Mediators of Inflammation |
| Online Access: | http://dx.doi.org/10.1080/09629350020025728 |
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| author | Sandra H. P. Farsky Luís Roberto C. Gonçalves José M. Gutiérrez Adriana P. Correa Alexandra Rucavado Philippe Gasque Denise V. Tambourgi |
| author_facet | Sandra H. P. Farsky Luís Roberto C. Gonçalves José M. Gutiérrez Adriana P. Correa Alexandra Rucavado Philippe Gasque Denise V. Tambourgi |
| author_sort | Sandra H. P. Farsky |
| collection | DOAJ |
| description | The venom of the snake Bothrops asper, the most important poisonous snake in Central America, evokes an inflammatory response, the mechanisms of which are not well characterized. The objectives of this study were to investigate whether B. asper venom and its purified toxins – phospholipases and
metalloproteinase – activate the complement system and the contribution of the effect on leucocyte recruitment.
In vitro chemotaxis assays were performed using Boyden's chamber model to investigate the ability of serum incubated with venom and its purified toxins to induce neutrophil migration. The complement consumption by the venom was evaluated using an in vitro haemolytic assay. The importance of complement activation by the venom on neutrophil migration was investigated in vivo by injecting the venom into the peritoneal cavity of C5-deficient mice. Data obtained demonstrated that serum incubated with crude venom and its purified metalloproteinase BaP–1 are able to induce rat neutrophil chemotaxis, probably mediated by agent(s) derived from the complement system. This hypothesis was corroborated by the capacity of the venom to activate this system in vitro. The involvement of C5a in neutrophil chemotaxis induced by venom-activated serum was demonstrated by abolishing migration when neutrophils were pre-incubated with antirat C5a receptor antibody. The relevance of the complement system in in vivo leucocyte mobilization was further demonstrated by the drastic decrease of this response in C5-deficient mice. Pre-incubation of serum with the soluble human recombinant complement receptor type 1 (sCR 1) did not prevent the response induced by the venom, but abolished the migration evoked by metalloproteinase-activated serum. These data show the role of the complement system in bothropic envenomation and the participation of metalloproteinase in the effect. Also, they suggest that the venom may contain other component(s) which can cause direct activation of C5a. |
| format | Article |
| id | doaj-art-079962fb77fe48c396934fd8523aa36e |
| institution | Kabale University |
| issn | 0962-9351 1466-1861 |
| language | English |
| publishDate | 2000-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Mediators of Inflammation |
| spelling | doaj-art-079962fb77fe48c396934fd8523aa36e2025-02-03T01:27:31ZengWileyMediators of Inflammation0962-93511466-18612000-01-019521322110.1080/09629350020025728Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitmentSandra H. P. Farsky0Luís Roberto C. Gonçalves1José M. Gutiérrez2Adriana P. Correa3Alexandra Rucavado4Philippe Gasque5Denise V. Tambourgi6Laboratory of Immunochemistry, Institute Butantan, Av. Vital Brazil, 1500 São Paulo, São Paulo, SP 05503–900, BrazilLaboratory of Pathophysiology, Institute Butantan, Av. Vital Brazil, 1500 São Paulo, São Paulo, SP 05503–900, BrazilInstitute Clodomiro Picado, Faculty of Microbiology, University of Costa Rica, San José, Costa RicaLaboratory of Immunochemistry, Institute Butantan, Av. Vital Brazil, 1500 São Paulo, São Paulo, SP 05503–900, BrazilInstitute Clodomiro Picado, Faculty of Microbiology, University of Costa Rica, San José, Costa RicaBrain Inflammation and Immunity Group, Department of Medical Biochemistry, University of Wales College of Medicine, Cardiff, UKLaboratory of Immunochemistry, Institute Butantan, Av. Vital Brazil, 1500 São Paulo, São Paulo, SP 05503–900, BrazilThe venom of the snake Bothrops asper, the most important poisonous snake in Central America, evokes an inflammatory response, the mechanisms of which are not well characterized. The objectives of this study were to investigate whether B. asper venom and its purified toxins – phospholipases and metalloproteinase – activate the complement system and the contribution of the effect on leucocyte recruitment. In vitro chemotaxis assays were performed using Boyden's chamber model to investigate the ability of serum incubated with venom and its purified toxins to induce neutrophil migration. The complement consumption by the venom was evaluated using an in vitro haemolytic assay. The importance of complement activation by the venom on neutrophil migration was investigated in vivo by injecting the venom into the peritoneal cavity of C5-deficient mice. Data obtained demonstrated that serum incubated with crude venom and its purified metalloproteinase BaP–1 are able to induce rat neutrophil chemotaxis, probably mediated by agent(s) derived from the complement system. This hypothesis was corroborated by the capacity of the venom to activate this system in vitro. The involvement of C5a in neutrophil chemotaxis induced by venom-activated serum was demonstrated by abolishing migration when neutrophils were pre-incubated with antirat C5a receptor antibody. The relevance of the complement system in in vivo leucocyte mobilization was further demonstrated by the drastic decrease of this response in C5-deficient mice. Pre-incubation of serum with the soluble human recombinant complement receptor type 1 (sCR 1) did not prevent the response induced by the venom, but abolished the migration evoked by metalloproteinase-activated serum. These data show the role of the complement system in bothropic envenomation and the participation of metalloproteinase in the effect. Also, they suggest that the venom may contain other component(s) which can cause direct activation of C5a.http://dx.doi.org/10.1080/09629350020025728 |
| spellingShingle | Sandra H. P. Farsky Luís Roberto C. Gonçalves José M. Gutiérrez Adriana P. Correa Alexandra Rucavado Philippe Gasque Denise V. Tambourgi Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment Mediators of Inflammation |
| title | Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment |
| title_full | Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment |
| title_fullStr | Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment |
| title_full_unstemmed | Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment |
| title_short | Bothrops asper snake venom and its metalloproteinase BaP–1 activate the complement system. Role in leucocyte recruitment |
| title_sort | bothrops asper snake venom and its metalloproteinase bap 1 activate the complement system role in leucocyte recruitment |
| url | http://dx.doi.org/10.1080/09629350020025728 |
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