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

Abstract

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 NH(2)-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.

• Authors: María E Peichoto, Stephen P Mackessy, Pamela Teibler, Flávio L Tavares, Paula L Burckhardt, María C Breno, Ofelia Acosta, Marcelo L Santoro
• Journal: Comparative biochemistry and physiology. Toxicology & pharmacology : CBP (Comp Biochem Physiol C Toxicol Pharmacol) Vol. 150 Issue 1 Pg. 79-84 (Jul 2009) ISSN: 1532-0456 [Print] United States
• PMID: 19285568 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Membrane Glycoproteins
• Snake Venoms

Topics

• Amino Acid Sequence
• Animals
• Male
• Membrane Glycoproteins (genetics, isolation & purification, toxicity)
• Mice
• Molecular Sequence Data
• Muscle, Skeletal (drug effects, pathology)
• Rats
• Rats, Wistar
• Snake Venoms (genetics, isolation & purification, toxicity)