Inflammatory events induced by Lys-49 and Asp-49 phospholipases A2 isolated from Bothrops asper snake venom: role of catalytic activity

Zuliani, Juliana Pavan; Fernandes, C.M.; Zamunér, Stella Regina; Gutiérrez, José Marı́a; Teixeira, Catarina

doi:10.1016/j.toxicon.2004.11.004

Cited by 112 publications

(93 citation statements)

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“…(Oliveira et al, 2008) and induced cytotoxicity in a primary cell culture of rat hippocampal neurons (de Carvalho et al, 2014). Many venom PLA2s have been shown to induce inflammation characterized by increase of vascular permeability (Zuliani et al, 2005a, Corasolla Carregari et al, 2013, edema formation (Ferreira et al, 2013, Kumar et al, 2015, and recruitment and activation of leukocytes (Zuliani et al, 2005b, Moreira et al, 2011.…”

Section: Discussionmentioning

confidence: 99%

Lemnitoxin, the major component of Micrurus lemniscatus coral snake venom, is a myotoxic and pro-inflammatory phospholipase A2

et al. 2016

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Section: Discussionmentioning

confidence: 99%

Lemnitoxin, the major component of Micrurus lemniscatus coral snake venom, is a myotoxic and pro-inflammatory phospholipase A2

et al. 2016

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“…When comparing exudate proteomics from mice injected with a PI hemorrhagic SVMP to that from tissue injected with a myotoxic PLA 2 , higher amounts of types I and III collagens were found with the latter. Myotoxic PLA 2 s induce muscle necrosis of rapid onset by damaging the integrity of muscle fiber plasma membrane [106] and induce inflammation characterized by pain, edema, synthesis of cytokines and MMPs, and a prominent cellular infiltrate [103,107,108]. Thus, it is suggested that the hydrolysis of fibrillar collagens is a consequence of the action of endogenous MMPs and perhaps other proteinases derived from resident and inflammatory cells.…”

Section: Action Of Svmps On Fibrillar Collagens: a Secondary Outcomentioning

confidence: 99%

A Comprehensive View of the Structural and Functional Alterations of Extracellular Matrix by Snake Venom Metalloproteinases (SVMPs): Novel Perspectives on the Pathophysiology of Envenoming

Gutiérrez

Escalante

Rucavado

et al. 2016

Toxins

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Snake venom metalloproteinases (SVMPs) affect the extracellular matrix (ECM) in multiple and complex ways. Previously, the combination of various methodological platforms, including electron microscopy, histochemistry, immunohistochemistry, and Western blot, has allowed a partial understanding of such complex pathology. In recent years, the proteomics analysis of exudates collected in the vicinity of tissues affected by SVMPs has provided novel and exciting information on SVMP-induced ECM alterations. The presence of fragments of an array of ECM proteins, including those of the basement membrane, has revealed a complex pathological scenario caused by the direct action of SVMPs. In addition, the time-course analysis of these changes has underscored that degradation of some fibrillar collagens is likely to depend on the action of endogenous proteinases, such as matrix metalloproteinases (MMPs), synthesized as a consequence of the inflammatory process. The action of SVMPs on the ECM also results in the release of ECM-derived biologically-active peptides that exert diverse actions in the tissue, some of which might be associated with reparative events or with further tissue damage. The study of the effects of SVMP on the ECM is an open field of research which may bring a renewed understanding of snake venom-induced pathology.

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“…The venoms from these viperids contain phospholipases A 2 (PLA 2 ) that hydrolyze phospholipids at the sn-2 position in a calcium-dependent manner, releasing fatty acids and lysophospholipids (2). PLA 2 is the main enzyme responsible for signs and symptoms observed in crotalic envenomation, while it is only partially involved in manifestations of bothropic envenomation (3)(4)(5).…”

Section: Introductionmentioning

confidence: 99%

IgG antibodies against phospholipase A2 from Crotalus durissus terrificus: cross-reaction with venoms from Bothrops species from Argentina

Rodríguez¹,

Marzi²,

Maruñak³

et al. 2009

J. Venom. Anim. Toxins incl. Trop. Dis

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ABSTRACT:We examined the ability of IgG anti-crotalic PLA 2 to cross-react with Bothrops spp. venoms, from snakes found in the northeast of Argentina. Immunoblotting and ELISA tests showed that IgG anti-crotalic PLA 2 recognize antigens of bothropic venoms. Indirect hemolytic activity tests showed that the quantity of antibodies that neutralized 50% of Crotalus durissus terrificus venom (ED 50 : 2.1 mg IgG anti-crotalic PLA 2 /100 μg of venom) were also able to neutralize venom from other snakes in the following proportion: 34% of B. alternatus, 18% of B. diporus and 12% of B. jararacussu. Likewise, direct PLA2 activity neutralization tests showed a similar cross-neutralization pattern including 56% of B. alternatus, 29% of B. diporus and 30% of B. jararacussu. In addition, in a myotoxic activity neutralization test, measured by plasma activity of creatine kinase, 35% of B. alternatus venom and 26% of B. diporus venom were neutralized, while no neutralization was detected with B. jararacussu venom. This study presents original data concerning cross-reactions between bothropic venoms from Argentina and IgG anti-crotalic PLA 2 . Our results suggest that anti-crotalic PLA 2 antibodies should not be used to neutralize PLA 2 activity of B. alternatus, B. diporus and especially B. jararacussu venoms; nor to enrich commercial antivenoms against these Bothrops species.

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Inflammatory events induced by Lys-49 and Asp-49 phospholipases A2 isolated from Bothrops asper snake venom: role of catalytic activity

Cited by 112 publications

References 50 publications

Lemnitoxin, the major component of Micrurus lemniscatus coral snake venom, is a myotoxic and pro-inflammatory phospholipase A2

Lemnitoxin, the major component of Micrurus lemniscatus coral snake venom, is a myotoxic and pro-inflammatory phospholipase A2

A Comprehensive View of the Structural and Functional Alterations of Extracellular Matrix by Snake Venom Metalloproteinases (SVMPs): Novel Perspectives on the Pathophysiology of Envenoming

IgG antibodies against phospholipase A2 from Crotalus durissus terrificus: cross-reaction with venoms from Bothrops species from Argentina

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