Isolation and biochemical characterization of a γ-type phospholipase A2 inhibitor from Crotalus durissus collilineatus snake serum

Gimenes, Sarah Natalie Cirilo; Ferreira, Francis Barbosa; Silveira, Ana Carolina Portella; Rodrigues, Renata Santos; Yoneyama, Kelly Aparecida Geraldo; Santos, Jorge M.; Fontes, Marcos R.M.; Brites, Vera Lucia de Campos; Santos, André Luíz Quagliatto; Borges, Márcia Helena; Lopes, Daiana Silva; Rodrigues, Veridiana M.

doi:10.1016/j.toxicon.2014.01.012

Cited by 25 publications

(45 citation statements)

References 36 publications

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“…Their amino acid sequences contain two sets of standards cysteine residues, responsible for the formation of the three-finger motif [51]. This type of inhibitor has been reported in different snakes, as Crotalus durissus terrificus [52–54], Naja naja kaouthia [55, 56], Agkistrodon blomhoffii siniticus [57], Trimeresurus flavoviridis [58], Laticauda semifasciata [59], Elaphe quadrivirgata [60] , E. climacophora [50], Cerrophidion godmani [32], Notechis ater , Notechis ater serventyi [61], Oxyuranus scutellatus and O. microlepidotus [61], Pseudonaja textilis [61], Python reticulates [62], Notechis scutatus [63], Lachesis muta muta [64], Protobothrops flavoviridis [65], Bothrops alternatus, B. erythromelas, B. jararaca, B. moojeni, B. neuwiedi [51], Bothrops jararacussu [39] and Crotalus durissus collilineatus [66] and these γPLIs appear to be less specific, since they inhibit PLA 2 from groups I, II and III.…”

Section: Pla2 Inhibitory Proteins (Plis) From Snake Bloodmentioning

confidence: 99%

Alpha-type phospholipase A2 inhibitors from snake blood

Santos-Filho

Santos

2017

J Venom Anim Toxins Incl Trop Dis

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It is of popular and scientific knowledge that toxins from snake venom (among them the PLA2 and myotoxins) are neutralized by various compounds, such as antibodies and proteins purified from animal blood. Venomous and nonvenomous snakes have PLA2 inhibitory proteins, called PLIs, in their blood serum. One hypothesis that could explain the presence of these PLIs in the serum of venomous snakes would be self-protection against the enzymes of their own venom, which eventually could reach the circulatory system. However, the presence of PLIs in non-venomous snakes suggests that their physiological role might not be restricted to protection against PLA2 toxins, but could be extended to other functions, as in the innate immune system and local regulation of PLA2s. The present study aimed to review the currently available literature on PLA2 and myotoxin alpha inhibitors present in snake plasma, thus helping to improve the research on these molecules. Furthermore, this review includes current information regarding the mechanism of action of these inhibitors in an attempt to better understand their application, and proposes the use of these molecules as new models in snakebite therapy. These molecules may help in the neutralization of different types of phospholipases A2 and myotoxins, complementing the conventional serum therapy.

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Section: Pla2 Inhibitory Proteins (Plis) From Snake Bloodmentioning

confidence: 99%

Alpha-type phospholipase A2 inhibitors from snake blood

Santos-Filho

Santos

2017

J Venom Anim Toxins Incl Trop Dis

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“…Creatine kinase levels, which reflects myotoxicity, were also reduced when PLA 2 s were incubated with the inhibitor (Fig 4C). Other γPLIs from venomous and non-venomous snakes also demonstrated the inhibitory potential in the pharmacological activities caused by PLA 2 [30,38,40]. In addition, our data showed no statistical differences of Gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictor.…”

Section: Resultsmentioning

confidence: 44%

“…BoaγPLI secondary structure was investigated by circular dichroism (Fig 3B), presenting 21.4% of alpha-helices, 39.4% of beta-sheets and 38.7% of random coils. Besides that, incubation of BoaγPLI with Asp-49 and Lys-49 PLA 2 s does not significantly alter the spectrum shown in circular dichroism, which was also evidenced in γCdcPLI and γBjussuMIP [38,40]. This observation suggests a weak interaction of BoaγPLI with PLA 2 , most likely non-covalently.…”

Section: Resultsmentioning

confidence: 59%

“…In comparison, the purification of the γPLI from Bothrops jararaca (γBjPLI) presented 1% of recovery, using the same methodology applied in this case [30], while under different approaches the γPLI from Crotalus durissus collilineatus (γCdcPLI) presented 2.69% [38]. The higher recovery of PLIs from venomous snakes may be related to the constant contact with the venom, which may stimulate the presence of inhibitors in the plasma [39].…”

Section: Resultsmentioning

confidence: 96%

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BoaγPLI: Structural and functional characterization of the gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictor

et al. 2020

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Plasma in several organisms has components that promote resistance to envenomation by inhibiting specific proteins from snake venoms, such as phospholipases A 2 (PLA 2 s). The major hypothesis for inhibitor's presence would be the protection against self-envenomation in venomous snakes, but the occurrence of inhibitors in non-venomous snakes and other animals has opened new perspectives for this molecule. Thus, this study showed for the first time the structural and functional characterization of the PLA 2 inhibitor from the Boa constrictor serum (BoaγPLI), a non-venomous snake that dwells extensively the Brazilian territory. Therefore, the inhibitor was isolated from B. constrictor serum, with 0.63% of recovery. SDS-PAGE showed a band at~25 kDa under reducing conditions and~20 kDa under non-reducing conditions. Chromatographic analyses showed the presence of oligomers formed by BoaγPLI. Primary structure of BoaγPLI suggested an estimated molecular mass of 22 kDa. When BoaγPLI was incubated with Asp-49 and Lys-49 PLA 2 there was no severe change in its dichroism spectrum, suggesting a non-covalent interaction. The enzymatic assay showed a dose-dependent inhibition, up to 48.2%, when BoaγPLI was incubated with Asp-49 PLA 2 , since Lys-49 PLA 2 has a lack of enzymatic activity. The edematogenic and myotoxic effects of PLA 2 s were also inhibited by BoaγPLI. In summary, the present work provides new insights into inhibitors from non-venomous snakes, which possess PLIs in their plasma, although the contact with venom is unlikely. OPEN ACCESS Citation: Rodrigues CFB, Serino-Silva C, Morais-Zani Kd, Kavazoi VK, Carvalho MPN, Grego KF, et al. (2020) BoaγPLI: Structural and functional characterization of the gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictor. PLoS ONE 15(2): e0229657. https://doi.org/10.

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“…)[22], [61] Bothrops neuwiedi Jararaca pintada (Port. )[61] Cerrophidion godmani Honduras montane pit viper[21] Crotalus durissus collilineatus Brazilian rattlesnake[71] Crotalus durissus terrificus South American rattlesnake, tropical rattlesnake[51–53] Lachesis muta South American bushmaster[72] Gloydius brevicaudus Short-tailed mamushi, Japanese mamushi or Chinese mamushi[73] Protobothrops flavoviridis Habu[25] Protobothrops elegans Sakishima habu[41] a Recombinant homolog …”

Section: Gamma Class Of Sbplis (Sbγplis)mentioning

confidence: 99%

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Campos-Júnior

Melo

Dias

et al. 2016

J Venom Anim Toxins Incl Trop Dis

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The blood plasma of numerous snake species naturally comprises endogenous phospholipase A2 inhibitors, which primarily neutralize toxic phospholipases A2 that may eventually reach their circulation. This inhibitor type is generally known as snake blood phospholipase A2 inhibitors (sbPLIs). Most, if not all sbPLIs are oligomeric glycosylated proteins, although the carbohydrate moiety may not be essential for PLA2 inhibition in every case. The presently known sbPLIs belong to one of three structural classes – namely sbαPLI, sbβPLI or sbγPLI – depending on the presence of characteristic C-type lectin-like domains, leucine-rich repeats or three-finger motifs, respectively. Currently, the most numerous inhibitors described in the literature are sbαPLIs and sbγPLIs, whereas sbβPLIs are rare. When the target PLA2 is a Lys49 homolog or an Asp49 myotoxin, the sbPLI is denominated a myotoxin inhibitor protein (MIP). In this brief overview, the most relevant data on sbPLIs will be presented. Representative examples of sbαPLIs and sbγPLIs from two Old World – Gloydius brevicaudus and Malayopython reticulatus – and two New World – Bothrops alternatus and Crotalus durissus terrificus – snake species will be emphasized.

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Isolation and biochemical characterization of a γ-type phospholipase A2 inhibitor from Crotalus durissus collilineatus snake serum

Cited by 25 publications

References 36 publications

Alpha-type phospholipase A2 inhibitors from snake blood

Alpha-type phospholipase A2 inhibitors from snake blood

BoaγPLI: Structural and functional characterization of the gamma phospholipase A2 plasma inhibitor from the non-venomous Brazilian snake Boa constrictor

Endogenous phospholipase A2 inhibitors in snakes: a brief overview

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