Isolation and functional characterization of a new myotoxic acidic phospholipase A2 from Bothrops pauloensis snake venom

Rodrigues, Renata Santos; Izidoro, Luíz Fernando Moreira; Teixeira, Sabrina S.; Silveira, Lucas B.; Hamaguchi, Amélia; Homsi-Brandeburgo, Maria Inês; Selistre-de-Araújo, Heloísa Sobreiro; Giglio, José Roberto; Fuly, André Lopes; Soares, Andreimar M.; Rodrigues, Veridiana M.

doi:10.1016/j.toxicon.2007.03.005

Cited by 60 publications

(46 citation statements)

References 41 publications

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“…Similar results were found with BmooTX-I obtained from B. moojeni, in which extensive cellular destruction and abundant leukocitary infiltrate were described and, further displaying contracted and clumped fibers in different stages of degeneration [15]. Bp-PLA2 from B. pauloensis [14], whose myotoxicity was confirmed by the increase in the CK activity was similar to induced by whole venom. In the same way, BinTX-I from B. insularis, also increased CK activity.…”

Section: Discussionsupporting

confidence: 84%

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A Novel Acidic Myotoxic Phospholipase A2 of Colombian B. asper Venom. Isolation and Functional Characterization

Arias¹,

Rey-Suárez²,

Jiménez³

et al. 2017

Preprint

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Section: Discussionsupporting

confidence: 84%

“…Additionally, with B. pauloensis [14] and from B. moojeni [15] PLA2s, which it was only had been reported the N-Terminal, and were not included in the lining.…”

Section: Discussionmentioning

confidence: 99%

A Novel Acidic Myotoxic Phospholipase A2 of Colombian B. asper Venom. Isolation and Functional Characterization

Arias¹,

Rey-Suárez²,

Jiménez³

et al. 2017

Preprint

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“…These findings are consistent with observations in most of the acidic PLA 2 s purified from snake venoms, which generally lack myotoxicity. However, some recently isolated acidic PLA 2 s display myotoxicity in vivo [14,20,21,40,47]. Although it is clear that the catalytic activity of PLA 2 s is not a sufficient requirement to generate myotoxicity per se, the structural determinants of such differences in myotoxicity among acidic enzymes are unknown, and their identification poses a challenging question.…”

Section: Discussionmentioning

confidence: 99%

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

et al. 2010

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a b s t r a c tPhospholipases A 2 (PLA 2 ) are major components of snake venoms, exerting a variety of relevant toxic actions such as neurotoxicity and myotoxicity, among others. Since the majority of toxic PLA 2 s are basic proteins, acidic isoforms and their possible roles in venoms are less understood. In this study, an acidic enzyme (BaspPLA 2 -II) was isolated from the venom of Bothrops asper (Pacific region of Costa Rica) and characterized. BaspPLA 2 -II is monomeric, with a mass of 14,212 AE 6 Da and a pI of 4.9. Its complete sequence of 124 amino acids was deduced through cDNA and protein sequencing, showing that it belongs to the Asp49 group of catalytically active enzymes. In vivo and in vitro assays demonstrated that BaspPLA 2 -II, in contrast to the basic Asp49 counterparts present in the same venom, lacks myotoxic, cytotoxic, and anticoagulant activities. BaspPLA 2 -II also differed from other acidic PLA 2 s described in Bothrops spp. venoms, as it did not show hypotensive and anti-platelet aggregation activities. Furthermore, this enzyme was not lethal to mice at intravenous doses up to 100 mg (5.9 mg/g), indicating its lack of neurotoxic activity. The only toxic effect recorded in vivo was a moderate induction of local edema. Therefore, the toxicological characteristics of BaspPLA 2 -II suggest that it does not play a key role in the pathophysiology of envenomings by B. asper, and that its purpose might be restricted to digestive functions. Immunochemical analyses using antibodies raised against BaspPLA 2 -II revealed that acidic and basic PLA 2 s form two different antigenic groups in B. asper venom.

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“…Directly, it is possible to detect the presence of PLA2s with the use of chromogenic substrates, such as 4N3OBA(4-nitro-3-octanoyloxybenzoic acid) that induce the formation of detectable product at 425 nm [65] and fluorescent substrates (NBD) coupled to phospholipids that are used to quantitively and qualitatively survey the PLA2s activity isolated from snake venom [23].…”

Section: Functional Characterizationmentioning

confidence: 99%

“…On the other hand, acid PLA2s present in Bothrops snake venoms were not studied as well as basic PLA2s, resulting in little knowledge regarding the action mechanism of these enzymes [21][22][23][24][25].…”

Section: Introductionmentioning

confidence: 99%

Purification of Phospholipases A2 from American Snake Venoms

Stábeli¹,

Simões-Silva²,

Kayano³

et al. 2012

Chromatography - The Most Versatile Method of Chemical Analysis

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Isolation and functional characterization of a new myotoxic acidic phospholipase A2 from Bothrops pauloensis snake venom

Cited by 60 publications

References 41 publications

A Novel Acidic Myotoxic Phospholipase A<sub>2</sub> of Colombian <em>B. asper</em> Venom. Isolation and Functional Characterization

A Novel Acidic Myotoxic Phospholipase A<sub>2</sub> of Colombian <em>B. asper</em> Venom. Isolation and Functional Characterization

Isolation of an acidic phospholipase A2 from the venom of the snake Bothrops asper of Costa Rica: Biochemical and toxicological characterization☆

Purification of Phospholipases A2 from American Snake Venoms

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