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


ABSTRACT:

Background

Endogenous phospholipase A2 inhibitors from snake blood (sbPLIs) have been isolated from several species around the world, with the primary function of self-protection against the action of toxic phospholipases A2. 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 non-venomous snake species from America.

Methods

PLA2 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 sb?PLI 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 PLA2 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 sb?PLIs from the literature.

Results

The blood plasma of B. constrictor displayed PLA2 inhibitory activity. A CNF-like 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 PLA2 inhibition. BcNF showed highest identity scores (ISs) with sb?PLIs 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 sb?PLI (BcNF) was described in the blood plasma of B. constrictor. BcNF displayed higher primary identity with sb?PLIs from Viperidae than to sb?PLIs from non-venomous species from Asia. The physiological role played by sb?PLIs in non-venomous snake species remains to be understood. Further investigation is needed.

SUBMITTER: Fortes-Dias CL 

PROVIDER: S-EPMC7092641 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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Identification and characterization of the first endogenous phospholipase A<sub>2</sub> inhibitor from a non-venomous tropical snake, <i>Boa constrictor</i> (Serpentes: Boidae).

Fortes-Dias Consuelo L CL   Macedo Diego Henrique Fagundes DHF   Barbosa Rafaella Pereira RP   Souza-Silva Gabriel G   Ortolani Paula Ladeira PL  

The journal of venomous animals and toxins including tropical diseases 20200313


<h4>Background</h4>Endogenous phospholipase A<sub>2</sub> inhibitors from snake blood (sbPLIs) have been isolated from several species around the world, with the primary function of self-protection against the action of toxic phospholipases A<sub>2.</sub> 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 <i>Boa constrictor</i> (popularly known as <i>jiboia</i>), a non-venomous snake species fr  ...[more]

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