A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria
Autor(a) principal: | |
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Data de Publicação: | 2021 |
Outros Autores: | , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UFRGS |
Texto Completo: | http://hdl.handle.net/10183/253625 |
Resumo: | 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 aminoterminal 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 Grampositive 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. |
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Barros, Karina Margareti Alencar deSardi, Janaina de Cássia OrlandiNeto, Simone MariaMacedo, Alexandre JoséRamalho, Suellen RodriguesOliveira, Daniella Gorete Lourenço dePontes, Gemilson SoaresWeber, Simone SchneiderOliveira, Caio Fernando Ramalho deMacedo, Maria Lígia Rodrigues2023-01-12T04:58:35Z20210753-3322http://hdl.handle.net/10183/253625001157251Erythrina 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 aminoterminal 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 Grampositive 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.application/pdfengBiomedicine & pharmacotherapy. Paris. Vol. 144 (Dec. 2021), 112198, 11 p.Inibidores de proteasesAntibacterianosBiofilmesPeptidase inhibitorAdherenceErythrina poeppigianaAntibacterial activityAntibiofilm activityA new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteriaEstrangeiroinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da UFRGSinstname:Universidade Federal do Rio Grande do Sul (UFRGS)instacron:UFRGSTEXT001157251.pdf.txt001157251.pdf.txtExtracted Texttext/plain64850http://www.lume.ufrgs.br/bitstream/10183/253625/2/001157251.pdf.txt8241696a7f3580ad7bbd0f0283c9005fMD52ORIGINAL001157251.pdfTexto completo (inglês)application/pdf1672452http://www.lume.ufrgs.br/bitstream/10183/253625/1/001157251.pdfedf5b67259f7fee55c79d7a01675ca05MD5110183/2536252023-01-13 06:04:20.347758oai:www.lume.ufrgs.br:10183/253625Repositório de PublicaçõesPUBhttps://lume.ufrgs.br/oai/requestopendoar:2023-01-13T08:04:20Repositório Institucional da UFRGS - Universidade Federal do Rio Grande do Sul (UFRGS)false |
dc.title.pt_BR.fl_str_mv |
A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria |
title |
A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria |
spellingShingle |
A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria Barros, Karina Margareti Alencar de Inibidores de proteases Antibacterianos Biofilmes Peptidase inhibitor Adherence Erythrina poeppigiana Antibacterial activity Antibiofilm activity |
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 |
A new Kunitz trypsin inhibitor from Erythrina poeppigiana exhibits antimicrobial and antibiofilm properties against bacteria |
author |
Barros, Karina Margareti Alencar de |
author_facet |
Barros, Karina Margareti Alencar de Sardi, Janaina de Cássia Orlandi Neto, Simone Maria Macedo, Alexandre José Ramalho, Suellen Rodrigues Oliveira, Daniella Gorete Lourenço de Pontes, Gemilson Soares Weber, Simone Schneider Oliveira, Caio Fernando Ramalho de Macedo, Maria Lígia Rodrigues |
author_role |
author |
author2 |
Sardi, Janaina de Cássia Orlandi Neto, Simone Maria Macedo, Alexandre José Ramalho, Suellen Rodrigues Oliveira, Daniella Gorete Lourenço de Pontes, Gemilson Soares Weber, Simone Schneider Oliveira, Caio Fernando Ramalho de Macedo, Maria Lígia Rodrigues |
author2_role |
author author author author author author author author author |
dc.contributor.author.fl_str_mv |
Barros, Karina Margareti Alencar de Sardi, Janaina de Cássia Orlandi Neto, Simone Maria Macedo, Alexandre José Ramalho, Suellen Rodrigues Oliveira, Daniella Gorete Lourenço de Pontes, Gemilson Soares Weber, Simone Schneider Oliveira, Caio Fernando Ramalho de Macedo, Maria Lígia Rodrigues |
dc.subject.por.fl_str_mv |
Inibidores de proteases Antibacterianos Biofilmes |
topic |
Inibidores de proteases Antibacterianos Biofilmes Peptidase inhibitor Adherence Erythrina poeppigiana Antibacterial activity Antibiofilm activity |
dc.subject.eng.fl_str_mv |
Peptidase inhibitor Adherence Erythrina poeppigiana Antibacterial activity Antibiofilm activity |
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 aminoterminal 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 Grampositive 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. |
publishDate |
2021 |
dc.date.issued.fl_str_mv |
2021 |
dc.date.accessioned.fl_str_mv |
2023-01-12T04:58:35Z |
dc.type.driver.fl_str_mv |
Estrangeiro info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10183/253625 |
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0753-3322 |
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001157251 |
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0753-3322 001157251 |
url |
http://hdl.handle.net/10183/253625 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.pt_BR.fl_str_mv |
Biomedicine & pharmacotherapy. Paris. Vol. 144 (Dec. 2021), 112198, 11 p. |
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openAccess |
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