Purification and characterization of a cysteine-rich secretory protein isolated from Philodryas patagoniensis snake venom

MARÍA ELISA PEICHOTO; STEPHEN P. MACKESSY; PAMELA TEIBLER; FLÁVIO LUIZ TAVARES; PAULA L. BURCKHARDT; MARÍA CRISTINA BRENO; OFELIA ACOSTA; MARCELO LARAMI SANTORO

COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. TOXICOLOGY & PHARMACOLOGY

Elsevier Science

Lugar: New York; Año: 2009 vol. 150 p. 79 - 84

1532-0456

Cysteine-rich secretory proteins (CRiSPs) are widespread in reptile venoms, but most have functions that remain unknown. In the present study we describe the purification and characterization of a CRiSP (patagonin) from the venom of the rear-fanged snake Philodryas patagoniensis, and demonstrate its biological activity. Patagonin is a single-chain protein, exhibiting a molecular mass of 24,858.6 Da, whose NH2-terminal and MS/MS-derived sequences are nearly identical to other snake venom CRiSPs. The purified protein hydrolyzed neither azocasein nor fibrinogen, and it could induce no edema, hemorrhage or inhibition of platelet adhesion and aggregation. In addition, patagonin did not inhibit contractions of rat aortic smooth muscle induced by high K+. However, it caused muscular damage to murine gastrocnemius muscle, an action that has not been previously described for any snake venom CRiSPs. Thus, patagonin will be important for studies of the structure-function and evolutionary relationships of this family of proteins that are widely distributed among snake venoms.