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Open AccessArticle

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

1
Postgraduate Program in Cellular and Molecular Biology—Federal University of Paraíba, João Pessoa, PB 58051-900, Brazil
2
S-Inova Biotech, Postgraduate Program in Biotechnology—Dom Bosco Catholic University, Campo Grande, MS 79117-010, Brazil
3
Protein Purification Laboratory and its Biological Functions, Faculty of Medicine, FAMED, Federal University of Mato Grosso do Sul (UFMS), Campo Grande, MS 79603-011, Brazil
4
Embrapa Beef Cattle, Campo Grande, MS 79106-550, Brazil
5
Center for Proteomic and Biochemical Analysis, Graduate Program in Genomic Sciences and Biotechnology, Catholic University of Brasilia, Brasilia 71966-700, Federal District, Brazil
6
Center of Biological and Health Sciences, Postgraduate Program in Science and Mathematics Education, Paraíba State University, Campina Grande PB 58429-500, Brazil
*
Author to whom correspondence should be addressed.
Toxins 2020, 12(9), 606; https://doi.org/10.3390/toxins12090606
Received: 2 July 2020 / Revised: 27 July 2020 / Accepted: 7 August 2020 / Published: 20 September 2020
(This article belongs to the Special Issue Application of Venom Phospholipase in the Treatment of Diseases)
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. View Full-Text
Keywords: bacterial resistance; animal venom; purification; antibacterial and antibiofilm activity bacterial resistance; animal venom; purification; antibacterial and antibiofilm activity
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MDPI and ACS Style

Nunes, E.; Frihling, B.; Barros, E.; de Oliveira, C.; Verbisck, N.; Flores, T.; de Freitas Júnior, A.; Franco, O.; de Macedo, M.; Migliolo, L.; Luna, K. Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom. Toxins 2020, 12, 606. https://doi.org/10.3390/toxins12090606

AMA Style

Nunes E, Frihling B, Barros E, de Oliveira C, Verbisck N, Flores T, de Freitas Júnior A, Franco O, de Macedo M, Migliolo L, Luna K. Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom. Toxins. 2020; 12(9):606. https://doi.org/10.3390/toxins12090606

Chicago/Turabian Style

Nunes, Ellynes; Frihling, Breno; Barros, Elizângela; de Oliveira, Caio; Verbisck, Newton; Flores, Taylla; de Freitas Júnior, Augusto; Franco, Octávio; de Macedo, Maria; Migliolo, Ludovico; Luna, Karla. 2020. "Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom" Toxins 12, no. 9: 606. https://doi.org/10.3390/toxins12090606

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