Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom

Abstract

Introduction: Bacterial resistance is a worldwide public health problem, requiring new therapeutic options. An alternative approach to this problem is the use of animal toxins isolated from snake venom, such as phospholipases A2 (PLA2), which have important antimicrobial activities. Bothropserythromelas is one of the snake species in the northeast of Brazil that attracts great medical-scientific interest. Here, we aimed to purify and characterize a PLA2 from B. erythromelas, searching for heterologous activities against bacterial biofilms. Methods: Venom extraction and quantification were followed by reverse-phase high-performance liquid chromatography (RP-HPLC) in C18 column, matrix-assisted ionization time-of-flight (MALDI-ToF) mass spectrometry, and sequencing by Edman degradation. All experiments were monitored by specific activity using a 4-nitro-3-(octanoyloxy) benzoic acid (4N3OBA) substrate. In addition, hemolytic tests and antibacterial tests including action against Escherichiacoli, Staphylococcusaureus, and Acinetobacterbaumannii were carried out. Moreover, tests of antibiofilm action against A. baumannii were also performed. Results: PLA2, after one purification step, presented 31 N-terminal amino acid residues and a molecular weight of 13.6564 Da, with enzymatic activity confirmed in 0.06 µM concentration. Antibacterial activity against S. aureus (IC50 = 30.2 µM) and antibiofilm activity against A. baumannii (IC50 = 1.1 µM) were observed. Conclusions: This is the first time that PLA2 purified from B. erythromelas venom has appeared as an alternative candidate in studies of new antibacterial medicines.

Purification, Characterization and Evaluation of the Antitumoral Activity of a Phospholipase A2 from the Snake Bothrops moojeni

“…The amino-terminal sequencing of BmPLA2 showed homology with other snake PLA 2 , sharing the highest identity with BmooPLA2. These two types of PLA 2 differed only by three amino acids: Phe 1 , Lys 2 and Met 19 , which in BmPLA2 corresponded to Asn 1 , Leu 2 and Leu 19 [25][26][27][28].…”

Imported Pet Reptiles and Their “Blind Passengers”—In-Depth Characterization of 80 Acinetobacter Species Isolates

“…Interestingly, reptile β-defensins, toxin components, and peptides with antimicrobial and antibiofilm activity against A. baumannii and other MDR bacteria have been described as a component of the innate immune system in different species, which might represent promising treatment options, even in human infections, especially when outperforming human homologues [ 78 , 79 , 80 , 81 , 82 , 83 ]. Reptiles might also cope with facultative pathogenic bacterial loads by a higher activity of antimicrobial molecules that could, for instance, be found in snakes and water monitors inhabiting polluted environments [ 84 ].…”

Fractionation of Vipera berus berus Snake Venom and Detection of Bioactive Compounds Targeted to Blood Coagulation System

“…In particular, by inducing Treg cells, these enzymes can be effective as potential therapeutic agents in atherosclerosis [16]. Antibacterial activity is another promising feature of phospholipases [17,18].…”