Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.

Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a...

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Autores principales:	Brunna M Okubo, Osmar N Silva, Ludovico Migliolo, Diego G Gomes, William F Porto, Carla L Batista, Carmel S Ramos, Hortência H S Holanda, Simoni C Dias, Octavio L Franco, Susana E Moreno
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/fe828be601e3425ab148f3bd21294275
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spelling	oai:doaj.org-article:fe828be601e3425ab148f3bd212942752021-11-18T07:24:56ZEvaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.1932-620310.1371/journal.pone.0033639https://doaj.org/article/fe828be601e3425ab148f3bd212942752012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22438972/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a multifaceted mixture of peptides, proteins and inorganic components. L-amino oxidase (LAO) is a multifunctional enzyme that is able to develop different activities including antibacterial activity. In this study a novel LAO from Bothrops mattogrosensis (BmLAO) was isolated and biochemically characterized. Partial enzyme sequence showed full identity to Bothrops pauloensis LAO. Moreover, LAO here isolated showed remarkable antibacterial activity against Gram-positive and -negative bacteria, clearly suggesting a secondary protective function. Otherwise, no cytotoxic activities against macrophages and erythrocytes were observed. Finally, some LAO fragments (BmLAO-f1, BmLAO-f2 and BmLAO-f3) were synthesized and further evaluated, also showing enhanced antimicrobial activity. Peptide fragments, which are the key residues involved in antimicrobial activity, were also structurally studied by using theoretical models. The fragments reported here may be promising candidates in the rational design of new antibiotics that could be used to control resistant microorganisms.Brunna M OkuboOsmar N SilvaLudovico MiglioloDiego G GomesWilliam F PortoCarla L BatistaCarmel S RamosHortência H S HolandaSimoni C DiasOctavio L FrancoSusana E MorenoPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 3, p e33639 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Brunna M Okubo Osmar N Silva Ludovico Migliolo Diego G Gomes William F Porto Carla L Batista Carmel S Ramos Hortência H S Holanda Simoni C Dias Octavio L Franco Susana E Moreno Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.
description	Healthcare-associated infections (HAIs) are causes of mortality and morbidity worldwide. The prevalence of bacterial resistance to common antibiotics has increased in recent years, highlighting the need to develop novel alternatives for controlling these pathogens. Pitviper venoms are composed of a multifaceted mixture of peptides, proteins and inorganic components. L-amino oxidase (LAO) is a multifunctional enzyme that is able to develop different activities including antibacterial activity. In this study a novel LAO from Bothrops mattogrosensis (BmLAO) was isolated and biochemically characterized. Partial enzyme sequence showed full identity to Bothrops pauloensis LAO. Moreover, LAO here isolated showed remarkable antibacterial activity against Gram-positive and -negative bacteria, clearly suggesting a secondary protective function. Otherwise, no cytotoxic activities against macrophages and erythrocytes were observed. Finally, some LAO fragments (BmLAO-f1, BmLAO-f2 and BmLAO-f3) were synthesized and further evaluated, also showing enhanced antimicrobial activity. Peptide fragments, which are the key residues involved in antimicrobial activity, were also structurally studied by using theoretical models. The fragments reported here may be promising candidates in the rational design of new antibiotics that could be used to control resistant microorganisms.
format	article
author	Brunna M Okubo Osmar N Silva Ludovico Migliolo Diego G Gomes William F Porto Carla L Batista Carmel S Ramos Hortência H S Holanda Simoni C Dias Octavio L Franco Susana E Moreno
author_facet	Brunna M Okubo Osmar N Silva Ludovico Migliolo Diego G Gomes William F Porto Carla L Batista Carmel S Ramos Hortência H S Holanda Simoni C Dias Octavio L Franco Susana E Moreno
author_sort	Brunna M Okubo
title	Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.
title_short	Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.
title_full	Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.
title_fullStr	Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.
title_full_unstemmed	Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.
title_sort	evaluation of an antimicrobial l-amino acid oxidase and peptide derivatives from bothropoides mattogrosensis pitviper venom.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/fe828be601e3425ab148f3bd21294275
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Evaluation of an antimicrobial L-amino acid oxidase and peptide derivatives from Bothropoides mattogrosensis pitviper venom.

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