A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria

Erythrina poeppigiana belongs to Fabaceae family (subfamily Papillionoideae) and is commonly found in tropical and subtropical regions in Brazil. Herein, we described the purification and characterization of a new Kunitz-type inhibitor, obtained from E. poeppigiana seeds (EpTI). EpTI is composed by...

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Autores principales:	Karina Margareti Alencar de Barros, Janaina de Cássia Orlandi Sardi, Simone Maria-Neto, Alexandre José Macedo, Suellen Rodrigues Ramalho, Daniella Gorete Lourenço de Oliveira, Gemilson Soares Pontes, Simone Schneider Weber, Caio Fernando Ramalho de Oliveira, Maria Lígia Rodrigues Macedo
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Peptidase inhibitor Adherence Erythrina poeppigiana Antibacterial activity Antibiofilm activity Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/04bdf57bbec74286915039e945838ff0
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spelling	oai:doaj.org-article:04bdf57bbec74286915039e945838ff02021-11-14T04:28:39ZA new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria0753-332210.1016/j.biopha.2021.112198https://doaj.org/article/04bdf57bbec74286915039e945838ff02021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S0753332221009823https://doaj.org/toc/0753-3322Erythrina poeppigiana belongs to Fabaceae family (subfamily Papillionoideae) and is commonly found in tropical and subtropical regions in Brazil. Herein, we described the purification and characterization of a new Kunitz-type inhibitor, obtained from E. poeppigiana seeds (EpTI). EpTI is composed by three isoforms of identical amino-terminal sequences with a molecular weight ranging from 17 to 20 kDa. The physicochemical features showed by EpTI are common to Kunitz inhibitors, including the dissociation constant (13.1 nM), stability against thermal (37–100 °C) and pH (2–10) ranging, and the presence of disulfide bonds stabilizing its reactive site. Furthermore, we investigated the antimicrobial, anti-adhesion, and anti-biofilm properties of EpTI against Gram-positive and negative bacteria. The inhibitor showed antimicrobial activity with a minimum inhibitory concentration (MIC, 5–10 µM) and minimum bactericidal concentration (MBC) of 10 µM for Enterobacter aerogenes, Enterobacter cloacae, Klebsiella pneumoniae, Staphylococcus aureus, and Staphylococcus haemolyticus. The combination of EpTI with ciprofloxacin showed a marked synergistic effect, reducing the antibiotic concentration by 150%. The increase in crystal violet uptake for S. aureus and K. pneumoniae strains was approximately 30% and 50%, respectively, suggesting that the bacteria plasma membrane is targeted by EpTI. Treatment with EpTI at 1x and 10 x MIC significantly reduced the biofilm formation and prompted the disruption of a mature biofilm. At MIC/2, EpTI decreased the bacterial adhesion to polystyrene surface within 2 h. Finally, EpTI showed low toxicity in animal model Galleria mellonella. Given its antimicrobial and anti-biofilm properties, the EpTI sequence might be used to design novel drug prototypes.Karina Margareti Alencar de BarrosJanaina de Cássia Orlandi SardiSimone Maria-NetoAlexandre José MacedoSuellen Rodrigues RamalhoDaniella Gorete Lourenço de OliveiraGemilson Soares PontesSimone Schneider WeberCaio Fernando Ramalho de OliveiraMaria Lígia Rodrigues MacedoElsevierarticlePeptidase inhibitorAdherenceErythrina poeppigianaAntibacterial activityAntibiofilm activityTherapeutics. PharmacologyRM1-950ENBiomedicine & Pharmacotherapy, Vol 144, Iss , Pp 112198- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Peptidase inhibitor Adherence Erythrina poeppigiana Antibacterial activity Antibiofilm activity Therapeutics. Pharmacology RM1-950
spellingShingle	Peptidase inhibitor Adherence Erythrina poeppigiana Antibacterial activity Antibiofilm activity Therapeutics. Pharmacology RM1-950 Karina Margareti Alencar de Barros Janaina de Cássia Orlandi Sardi Simone Maria-Neto Alexandre José Macedo Suellen Rodrigues Ramalho Daniella Gorete Lourenço de Oliveira Gemilson Soares Pontes Simone Schneider Weber Caio Fernando Ramalho de Oliveira Maria Lígia Rodrigues Macedo A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
description	Erythrina poeppigiana belongs to Fabaceae family (subfamily Papillionoideae) and is commonly found in tropical and subtropical regions in Brazil. Herein, we described the purification and characterization of a new Kunitz-type inhibitor, obtained from E. poeppigiana seeds (EpTI). EpTI is composed by three isoforms of identical amino-terminal sequences with a molecular weight ranging from 17 to 20 kDa. The physicochemical features showed by EpTI are common to Kunitz inhibitors, including the dissociation constant (13.1 nM), stability against thermal (37–100 °C) and pH (2–10) ranging, and the presence of disulfide bonds stabilizing its reactive site. Furthermore, we investigated the antimicrobial, anti-adhesion, and anti-biofilm properties of EpTI against Gram-positive and negative bacteria. The inhibitor showed antimicrobial activity with a minimum inhibitory concentration (MIC, 5–10 µM) and minimum bactericidal concentration (MBC) of 10 µM for Enterobacter aerogenes, Enterobacter cloacae, Klebsiella pneumoniae, Staphylococcus aureus, and Staphylococcus haemolyticus. The combination of EpTI with ciprofloxacin showed a marked synergistic effect, reducing the antibiotic concentration by 150%. The increase in crystal violet uptake for S. aureus and K. pneumoniae strains was approximately 30% and 50%, respectively, suggesting that the bacteria plasma membrane is targeted by EpTI. Treatment with EpTI at 1x and 10 x MIC significantly reduced the biofilm formation and prompted the disruption of a mature biofilm. At MIC/2, EpTI decreased the bacterial adhesion to polystyrene surface within 2 h. Finally, EpTI showed low toxicity in animal model Galleria mellonella. Given its antimicrobial and anti-biofilm properties, the EpTI sequence might be used to design novel drug prototypes.
format	article
author	Karina Margareti Alencar de Barros Janaina de Cássia Orlandi Sardi Simone Maria-Neto Alexandre José Macedo Suellen Rodrigues Ramalho Daniella Gorete Lourenço de Oliveira Gemilson Soares Pontes Simone Schneider Weber Caio Fernando Ramalho de Oliveira Maria Lígia Rodrigues Macedo
author_facet	Karina Margareti Alencar de Barros Janaina de Cássia Orlandi Sardi Simone Maria-Neto Alexandre José Macedo Suellen Rodrigues Ramalho Daniella Gorete Lourenço de Oliveira Gemilson Soares Pontes Simone Schneider Weber Caio Fernando Ramalho de Oliveira Maria Lígia Rodrigues Macedo
author_sort	Karina Margareti Alencar de Barros
title	A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
title_short	A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
title_full	A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
title_fullStr	A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
title_full_unstemmed	A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
title_sort	new kunitz trypsin inhibitor from erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/04bdf57bbec74286915039e945838ff0
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A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria

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