Article (Scientific journals)
Bothrops snake venom L-amino acid oxidases impair biofilm formation of clinically relevant bacteria.
Alves de Melo Fernandes, Thales; Rafaella Costa, Tássia; de Paula Menezes, Ralciane et al.
2024In Toxicon, 238, p. 107569
Peer Reviewed verified by ORBi
 

Files


Full Text
Bothrops snake venom L.pdf
Author postprint (956.71 kB)
Download

All documents in ORBi are protected by a user license.

Send to



Details



Keywords :
Antibacterial activity; Bacterial infections; Biofilm; L-amino acid oxidases; Snake venom; Crotalid Venoms; L-Amino Acid Oxidase; Snake Venoms; Animals; L-Amino Acid Oxidase/pharmacology; L-Amino Acid Oxidase/chemistry; Staphylococcus aureus; Escherichia coli; Snake Venoms/chemistry; Bacteria; Biofilms; Crotalid Venoms/toxicity; Bothrops; Venomous Snakes; Bothrops jararacussu; Bothrops moojeni; Toxicology
Abstract :
[en] The present work addressed the abilities of two L-amino acid oxidases isolated from Bothrops moojeni (BmooLAAO-I) and Bothrops jararacussu (BjussuLAAO-II) snake venoms to control the growth and prevent the biofilm formation of clinically relevant bacterial pathogens. Upon S. aureus (ATCC BAA44) and S. aureus (clinical isolates), BmooLAAO-I (MIC = 0.12 and 0.24 μg/mL, respectively) and BjussuLAAO-II (MIC = 0.15 μg/mL) showed a potent bacteriostatic effect. Against E. coli (ATCC BAA198) and E. coli (clinical isolates), BmooLAAO-I (MIC = 15.6 and 62.5 μg/mL, respectively) and BjussuLAAO-II (MIC = 4.88 and 9.76 μg/mL, respectively) presented a lower extent effect. Also, BmooLAAO-I (MICB50 = 0.195 μg/mL) and BjussuLAAO-II (MICB50 = 0.39 μg/mL) inhibited the biofilm formation of S. aureus (clinical isolates) in 88% and 89%, respectively, and in 89% and 53% of E. coli (clinical isolates). Moreover, scanning electron microscopy confirmed that the toxins affected bacterial morphology by increasing the roughness of the cell surface and inhibited the biofilm formation. Furthermore, analysis of the tridimensional structures of the toxins showed that the surface-charge distribution presents a remarkable positive region close to the glycosylation motif, which is more pronounced in BmooLAAO-I than BjussuLAAO-II. This region may assist the interaction with bacterial and biofilm surfaces. Collectively, our findings propose that venom-derived antibiofilm agents are promising biotechnological tools which could provide novel strategies for biofilm-associated infections.
Disciplines :
Chemistry
Author, co-author :
Alves de Melo Fernandes, Thales ;  Laboratory of Biochemistry and Animal Toxins, Institute of Biotechnology, Federal University of Uberlândia, Uberlândia, MG, Brazil
Rafaella Costa, Tássia;  Laboratory of Biochemistry and Animal Toxins, Institute of Biotechnology, Federal University of Uberlândia, Uberlândia, MG, Brazil
de Paula Menezes, Ralciane ;  Laboratory of Antimicrobial Testing, Institute of Biomedical Science, Federal University of Uberlândia, Uberlândia, MG, Brazil
Arantes de Souza, Meliza;  Laboratory of Antimicrobial Testing, Institute of Biomedical Science, Federal University of Uberlândia, Uberlândia, MG, Brazil
Gomes Martins, Carlos Henrique;  Laboratory of Antimicrobial Testing, Institute of Biomedical Science, Federal University of Uberlândia, Uberlândia, MG, Brazil
Junior, Nilson Nicolau ;  Laboratory of Molecular Modeling, Institute of Biotechnology, Federal University of Uberlândia, Uberlândia, MG, Brazil
Gobbi Amorim, Fernanda ;  Mass Spectrometry Laboratory, MolSys RU, University of Liège, 4000 Liège, Belgium
Quinton, Loïc  ;  Université de Liège - ULiège > Département de chimie (sciences) > Chimie biologique
Polloni, Lorena;  Laboratory of Biochemistry and Animal Toxins, Institute of Biotechnology, Federal University of Uberlândia, Uberlândia, MG, Brazil
Teixeira, Samuel Cota;  Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Science, Federal University of Uberlândia, MG, Brazil
Amália Vieira Ferro, Eloisa ;  Laboratory of Immunophysiology of Reproduction, Institute of Biomedical Science, Federal University of Uberlândia, MG, Brazil
Soares, Andreimar Martins;  Laboratory of Biotechnology of Proteins and Bioactive Compounds in the Western Amazon (LABIOPROT), Oswaldo Cruz Foundation, FIOCRUZ Rondônia, Federal University of Rondônia (UNIR), And National Institute of Science and Technology of Epidemiology of the Western Amazon, INCT-EPIAMO, Porto Velho-RO, Brazil
de Melo Rodrigues Ávila, Veridiana ;  Laboratory of Biochemistry and Animal Toxins, Institute of Biotechnology, Federal University of Uberlândia, Uberlândia, MG, Brazil. Electronic address: veridiana@ufu.br
More authors (3 more) Less
Language :
English
Title :
Bothrops snake venom L-amino acid oxidases impair biofilm formation of clinically relevant bacteria.
Publication date :
01 February 2024
Journal title :
Toxicon
ISSN :
0041-0101
eISSN :
1879-3150
Publisher :
Elsevier, England
Volume :
238
Pages :
107569
Peer reviewed :
Peer Reviewed verified by ORBi
Funding text :
The authors gratefully acknowledge the financial support by Universidade Federal de Uberlândia ( UFU ), Conselho Nacional de Desenvolvimento Científico e Tecnológico ( CNPq ), Fundação de Amparo à Pesquisa do Estado de Minas Gerais ( FAPEMIG ) (grant number CBB – APQ-01401-17), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - Brasil ( CAPES ) and the National Institute of Science and Technology in Theranostics and Nanobiotechnology INCT-TeraNano- CNPq / CAPES / FAPEMIG (grant number CNPq-465,669/2014–0). The Q-Exactive mass spectrometer was funded by ERDF and the Walloon Region grant and Peaks X+ version Studio 10.5 software was funded by ERDF's grant: BIOMED HUB Technology Support (grant number 2.2.1/996).The authors gratefully acknowledge the financial support by Universidade Federal de Uberlândia (UFU), Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Fundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG) (grant number CBB – APQ-01401-17), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior - Brasil (CAPES) and the National Institute of Science and Technology in Theranostics and Nanobiotechnology INCT-TeraNano-CNPq/CAPES/FAPEMIG (grant number CNPq-465,669/2014–0). The Q-Exactive mass spectrometer was funded by ERDF and the Walloon Region grant and Peaks X+ version Studio 10.5 software was funded by ERDF's grant: BIOMED HUB Technology Support (grant number 2.2.1/996).
Available on ORBi :
since 08 January 2026

Statistics


Number of views
13 (0 by ULiège)
Number of downloads
20 (0 by ULiège)

Scopus citations®
 
6
Scopus citations®
without self-citations
4
OpenCitations
 
3
OpenAlex citations
 
7

Bibliography


Similar publications



Contact ORBi