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• Ferreira, FBarbosa
• Gomes, MSérgio Rocha
• de Souza, DLorena Naves
• Gimenes, SNatalie Cirilo
• Castanheira, LEulalio
• Borges, MHelena
• Rodrigues, RSantos
• Yoneyama, KAparecida Geraldo
• Brandeburgo, MInês Homsi
• Rodrigues, VM.
• [+] on Google Scholar
• Ferreira, FBarbosa
• Gomes, MSérgio Rocha
• de Souza, DLorena Naves
• Gimenes, SNatalie Cirilo
• Castanheira, LEulalio
• Borges, MHelena
• Rodrigues, RSantos
• Yoneyama, KAparecida Geraldo
• Brandeburgo, MInês Homsi
• Rodrigues, VM.
• [+] on PubMed
• Ferreira, FBarbosa
• Gomes, MSérgio Rocha
• de Souza, DLorena Naves
• Gimenes, SNatalie Cirilo
• Castanheira, LEulalio
• Borges, MHelena
• Rodrigues, RSantos
• Yoneyama, KAparecida Geraldo
• Brandeburgo, MInês Homsi
• Rodrigues, VM.

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Toxins 2013, 5(12), 2403-2419; doi:10.3390/toxins5122403

Article

Molecular Cloning and Pharmacological Properties of an Acidic PLA₂ from Bothrops pauloensis Snake Venom

Francis Barbosa Ferreira ¹, Mário Sérgio Rocha Gomes ^1,2, Dayane Lorena Naves de Souza ¹, Sarah Natalie Cirilo Gimenes ¹, Letícia Eulalio Castanheira ¹, Márcia Helena Borges ³, Renata Santos Rodrigues ¹, Kelly Aparecida Geraldo Yoneyama ¹, Maria Inês Homsi Brandeburgo ¹ and Veridiana M. Rodrigues ^1,*

¹ Institute of Genetics and Biochemistry, Federal University of Uberlândia, UFU, 38400902 Uberlândia-MG, Brazil ² Department of Chemical and Physical, State University of Southwest Bahia (UESB), 45506-210 Jequié-BA, Brazil ³ Ezequiel Dias Foundation, FUNED, 30510-010 Belo Horizonte-MG, Brazil

* Author to whom correspondence should be addressed.

Received: 14 August 2013; in revised form: 13 November 2013 / Accepted: 21 November 2013 / Published: 4 December 2013

Download PDF Full-Text [1026 KB, uploaded 4 December 2013 16:29 CET]

Abstract: In this work, we describe the molecular cloning and pharmacological properties of an acidic phospholipase A₂ (PLA₂) isolated from Bothrops pauloensis snake venom. This enzyme, denominated BpPLA₂-TXI, was purified by four chromatographic steps and represents 2.4% of the total snake venom protein content. BpPLA₂-TXI is a monomeric protein with a molecular mass of 13.6 kDa, as demonstrated by Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF) analysis and its theoretical isoelectric point was 4.98. BpPLA₂-TXI was catalytically active and showed some pharmacological effects such as inhibition of platelet aggregation induced by collagen or ADP and also induced edema and myotoxicity. BpPLA₂-TXI displayed low cytotoxicity on TG-180 (CCRF S 180 II) and Ovarian Carcinoma (OVCAR-3), whereas no cytotoxicity was found in regard to MEF (Mouse Embryonic Fibroblast) and Sarcoma 180 (TIB-66). The N-terminal sequence of forty-eight amino acid residues was determined by Edman degradation. In addition, the complete primary structure of 122 amino acids was deduced by cDNA from the total RNA of the venom gland using specific primers, and it was significantly similar to other acidic D49 PLA₂s. The phylogenetic analyses showed that BpPLA₂-TXI forms a group with other acidic D49 PLA₂s from the gender Bothrops, which are characterized by a catalytic activity associated with anti-platelet effects.

Keywords: Bothrops pauloensis; phospholipase A₂; molecular cloning

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