A New Phospholipase A₂ from Lachesis muta rhombeata: Purification, Biochemical and Comparative Characterization with Crotoxin B

• Published in: Protein and peptide letters Vol. 22; no. 9; p. 816
• Main Authors: Cordeiro, Francielle A, Perini, Tibério G K, Bregge-Silva, Cristiane, Cremonez, Caroline M, Rodrigues, Renata S, Boldrini-França, Johara, Bordon, Karla de C F, De Souza, Dayane L N, Ache, David C, de M Rodrigues, Veridiana, Dos Santos, Wagner F, Rosa, Jose C, Arantesa, Eliane C
• Format: Journal Article
• Language: English
• Published: Netherlands 2015
• Subjects: Amino Acid Sequence; Animals; Creatine Kinase - analysis; Creatine Kinase - metabolism; Crotoxin - chemistry; Edema - chemically induced; Male; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Muscle, Skeletal - drug effects; Muscle, Skeletal - pathology; Peptide Fragments - analysis; Phospholipases A2 - chemistry; Phospholipases A2 - isolation & purification; Phospholipases A2 - toxicity; Platelet Aggregation - drug effects; Reptilian Proteins - chemistry; Reptilian Proteins - isolation & purification; Reptilian Proteins - toxicity; Sequence Alignment; Viper Venoms - chemistry; Viperidae
• DOI: 10.2174/0929866522666150706112431
• EISSN: 1875-5305

Phospholipases A2 (PLA2s) are enzymes responsible for inflammatory effects, edema formation, myotoxicity, neurotoxicity and other manifestations from envenoming. In this paper we report the isolation and biochemical characterization of Lmr-PLA2, the first acidic PLA2 found in Lachesis muta rhombeata venom. Furthermore, this study compared biological effects of Lmr-PLA2 and crotoxin B (CB), a PLA2 from Crotalus durissus terrificus venom. Lmr-PLA2 was isolated by molecular exclusion and reversed phase chromatography. The purified enzyme showed a molecular mass of 13,975 Da, pI of 5.46 and its partial amino acid sequence showed a high identity with PLA2s already described in the literature. In addition, this enzyme possesses the residue D49 in its amino acid sequence, indicating that it is a catalytically active PLA2. Lmr-PLA2 presented high phospholipase activity and was able to inhibit platelet aggregation. Studies of biochemical characterization of new PLA2s, as Lmr-PLA2, are relevant since they help to clarify the structure-function relationship of this important class of toxins.