Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom
| العنوان: | Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom |
|---|---|
| المؤلفون: | N. V. Verbisck, Karla Luna, Ludovico Migliolo, Breno Emanuel Farias Frihling, Ellynes Nunes, Elizângela de Barros, Taylla Michelle de Oliveira Flores, Octavio L. Franco, Maria de Macedo, Augusto de Freitas Júnior, Caio Fernando Ramalho de Oliveira |
| المساهمون: | Ellynes Nunes, Breno Frihling, Elizângela Barros, Caio de Oliveira, NEWTON VALERIO VERBISCK, CNPGC, Taylla Flores, Augusto de Freitas Júnior, Octávio Franco, Maria de Macedo, Ludovico Migliolo, Karla Luna. |
| المصدر: | Toxins Volume 12 Issue 9 Toxins, Vol 12, Iss 606, p 606 (2020) Repositório Institucional da EMBRAPA (Repository Open Access to Scientific Information from EMBRAPA-Alice) Empresa Brasileira de Pesquisa Agropecuária (Embrapa) instacron:EMBRAPA |
| بيانات النشر: | Preprints, 2020. |
| سنة النشر: | 2020 |
| مصطلحات موضوعية: | purification, animal venom, Health, Toxicology and Mutagenesis, lcsh:Medicine, Venom, Bothrops erythromelas, Toxicology, Bacterial resistance, 03 medical and health sciences, antibacterial and antibiofilm activity, Purification, 030304 developmental biology, Antibacterial and antibiofilm activity, chemistry.chemical_classification, 0303 health sciences, Edman degradation, biology, lcsh:R, 030302 biochemistry & molecular biology, bacterial resistance, Antimicrobial, biology.organism_classification, animal_sciences_zoology, Enzyme, Animal venom, chemistry, Biochemistry, Snake venom, Specific activity, Antibacterial activity |
| الوصف: | 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 µ M concentration. Antibacterial activity against S. aureus (IC50 = 30.2 µ M) and antibiofilm activity against A. baumannii (IC50 = 1.1 µ M) 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. |
| وصف الملف: | application/pdf |
| اللغة: | English |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e933b26decf7fe4b5e50086a10896a1cTest |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....e933b26decf7fe4b5e50086a10896a1c |
| قاعدة البيانات: | OpenAIRE |
| الوصف غير متاح. |