Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Campos-Júnior, Paulo Henrique Almeida; Melo, Lutiana Amaral de; Dias, Gabriel Latorre Fortes; Fortes-Dias, Consuelo Latorre

doi:10.1186/s40409-016-0092-5

Cited by 34 publications

(23 citation statements)

References 71 publications

(93 reference statements)

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“…This work shows for the first time the structural and functional characterization of the Boaγ-PLI, a PLI from Boa constrictor, a non-venomous Brazilian snake. Contrasting with the number of PLIs isolated from venomous snakes [14,16], only a small number of this molecule were isolated from non-venomous snakes [19,22], suggesting that the PLI is not restricted to protection against self-envenomation, but it may be involved in other unknown physiological mechanisms that has yet to be determined [23].…”

Section: Resultsmentioning

confidence: 87%

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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Section: Resultsmentioning

confidence: 87%

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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“…SbγPLIs are the most widely distributed inhibitors among elapid and viperid species from the Old and New World [12,13,14]. Concerning non-venomous snakes, as far as we know, until now sbγPLIs were solely purified from Asian species [4,5,6,7,8,9].…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of the first endogenous phospholipase A2 inhibitor from a non-venomous tropical snake, Boa constrictor (Serpentes: Boidae)

Fortes-Dias

Macedo

Barbosa

et al. 2020

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

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Background: Endogenous phospholipase A 2 inhibitors from snake blood (sbPLIs) have been isolated from several species around the world, with the primary function of selfprotection against the action of toxic phospholipases A 2. In American snakes, sbPLIs were solely described in pit vipers, in which the natural protection role is justified. In this study, we described a sbPLI in Boa constrictor (popularly known as jiboia), a nonvenomous snake species from America. Methods: PLA 2 inhibitory activity was tested in the blood plasma of B. constrictor using C. d. terrificus venom as the enzyme source. Antibodies developed against CNF, a sbγPLI from Crotalus durissus terrificus, were used to investigate the presence of homologues in the blood plasma of B. constrictor. A CNF-like molecule with a PLA 2 inhibitory activity was purified by column chromatography. The encoding gene for the inhibitor was cloned from B. constrictor liver tissue. The DNA fragment was cloned, purified and sequenced. The deduced primary sequence of interest was aligned with known sbγPLIs from the literature. Results: The blood plasma of B. constrictor displayed PLA 2 inhibitory activity. A CNFlike molecule (named BcNF) was identified and purified from the blood plasma of B. constrictor. Basic properties such as molecular mass, composing amino acids, and pI were comparable, but BcNF displayed reduced specific activity in PLA 2 inhibition. BcNF showed highest identity scores (ISs) with sbγPLIs from pit vipers from Latin America (90-100%), followed by gamma inhibitors from Asian viperid (80-90%). ISs below 70% were obtained for BcNF and non-venomous species from Asia. Conclusion: A functional sbγPLI (BcNF) was described in the blood plasma of B. constrictor. BcNF displayed higher primary identity with sbγPLIs from Viperidae than to sbγPLIs from non-venomous species from Asia. The physiological role played by sbγPLIs in non-venomous snake species remains to be understood. Further investigation is needed.

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“…Snakes generally produce svPLA 2 inhibitors (PLI) as an innate immunity product for survival of their own species [ 19 ]. According to the structural features, snake PLI can be divided into α, β and γ types [ 20 ]. PLI-α and PLI-β are mainly distributed in Viperidae, and their inhibitory activities are mainly against their venom type II sPLA 2 [ 21 – 23 ].…”

Section: Introductionmentioning

confidence: 99%

“…PLI-γ is a relatively nonspecific inhibitor that can inhibit svPLA 2 subtypes I and II, bee venom, type III PLA 2 from lizard venom, and mammalian sPLA 2 (IB and IIA). PLIγs are widely found in the Elapidae, Hydrophiidae, Boidae and Colubridae snake families [ 20 , 24 – 28 ].…”

Section: Introductionmentioning

confidence: 99%

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Preparation of monoclonal antibodies against gamma-type phospholipase A2 inhibitors and immunodetection of these proteins in snake blood

Xiong

Sun

et al. 2017

J Venom Anim Toxins Incl Trop Dis

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BackgroundThe gamma-type phospholipase A2 inhibitor (PLIγ) is a natural protein commonly found in snake serum, which can neutralize pathophysiological effects of snake venom phospholipases A2. Therefore, this protein is a potential candidate to the development of a novel antivenom. To the best of our knowledge, there is no antibody currently available for PLIγ identification and characterization.MethodsBioinformatics prediction of epitope using DNAStar software was performed based on the sequence of Sinonatrix annularis PLIγ (SaPLIγ). The best epitope 151CPVLRLSNRTHEANRNDLIKVA172 was chosen and synthesized, and then conjugated to keyhole limpet hemocyanin and bovine serum albumin for use as an immunogen and plate-coating antigen, respectively.ResultsEighteen IgG anti-PLIγ mAb hybridoma cell strains were obtained, and all the mAbs had positive interaction with recombinant His6-PLIγ and natural SaPLIγ. Moreover, the mAb from 10E9 strain was also successfully used for the immunodetection of other snake serum PLIγs. cDNA sequence alignment of those PLIγs from different snake species showed that their epitope segments were highly homologous.ConclusionsThe successful preparation of anti-PLIγmAb is significant for further investigation on the relationship between the structure and function of PLIγs, as well as the interaction between PLIγs and PLA2s.

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Endogenous phospholipase A2 inhibitors in snakes: a brief overview

Cited by 34 publications

References 71 publications

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

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

Identification and characterization of the first endogenous phospholipase A2 inhibitor from a non-venomous tropical snake, Boa constrictor (Serpentes: Boidae)

Preparation of monoclonal antibodies against gamma-type phospholipase A2 inhibitors and immunodetection of these proteins in snake blood

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