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

Background: Endogenous phospholipase A 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 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 (popularly known as ), a non-venomous snake species from America.

Methods: PLA inhibitory activity was tested in the blood plasma of using venom as the enzyme source. Antibodies developed against CNF, a sbγPLI from were used to investigate the presence of homologues in the blood plasma of . A CNF-like molecule with a PLA inhibitory activity was purified by column chromatography. The encoding gene for the inhibitor was cloned from 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 displayed PLA inhibitory activity. A CNF-like molecule (named BcNF) was identified and purified from the blood plasma of . Basic properties such as molecular mass, composing amino acids, and pI were comparable, but BcNF displayed reduced specific activity in PLA 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 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.