Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity

Detalhes bibliográficos
Autor(a) principal: Oliveira, Hugo Alexandre Mendes
Data de Publicação: 2016
Outros Autores: Boas, Diana Patrícia Andrade Vilas, Mesnage, Stéphane, Kluskens, Leon, Lavigne, Rob, Sillankorva, Sanna, Secundo, Francesco, Azeredo, Joana
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/1822/41411
Resumo: The present study demonstrates the antibacterial potential of a phage endolysin against Gram-negative pathogens, particularly against multidrug resistant strains of Acinetobacter baumannii. We have cloned, heterologously expressed and characterized a novel endolysin (ABgp46) from Acinetobacter phage vb_AbaP_CEB1 and tested its antibacterial activity against several multidrug-resistant A. baumannii strains. LC-MS revealed that ABgp46 is an N-acetylmuramidase, that is also active over a broad pH range (4.0-10.0) and temperatures up to 50°C. Interestingly, ABgp46 has intrinsic and specific anti-A. baumannii activity, reducing multidrug resistant strains by up to 2 logs within 2 hours. By combining ABgp46 with several organic acids that act as outer membrane permeabilizing agents, it is possible to increase and broaden antibacterial activity to include other Gram-negative bacterial pathogens. In the presence of citric and malic acid, ABgp46 reduces A. baumannii below the detection limit (> 5 log) and more than 4 logs P. aeruginosa and Salmonella Typhimurium strains. Overall, this globular endolysin exhibits a broad and high activity against Gram-negative pathogens, that can be enhanced in presence of citric and malic acid, and be used in human and veterinary medicine.
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spelling Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activityAcinetobacter baumanniiPhage endolysinsMass spectrometryCircular dichroismAntibacterial activityCiências Agrárias::Biotecnologia Agrária e AlimentarScience & TechnologyThe present study demonstrates the antibacterial potential of a phage endolysin against Gram-negative pathogens, particularly against multidrug resistant strains of Acinetobacter baumannii. We have cloned, heterologously expressed and characterized a novel endolysin (ABgp46) from Acinetobacter phage vb_AbaP_CEB1 and tested its antibacterial activity against several multidrug-resistant A. baumannii strains. LC-MS revealed that ABgp46 is an N-acetylmuramidase, that is also active over a broad pH range (4.0-10.0) and temperatures up to 50°C. Interestingly, ABgp46 has intrinsic and specific anti-A. baumannii activity, reducing multidrug resistant strains by up to 2 logs within 2 hours. By combining ABgp46 with several organic acids that act as outer membrane permeabilizing agents, it is possible to increase and broaden antibacterial activity to include other Gram-negative bacterial pathogens. In the presence of citric and malic acid, ABgp46 reduces A. baumannii below the detection limit (> 5 log) and more than 4 logs P. aeruginosa and Salmonella Typhimurium strains. Overall, this globular endolysin exhibits a broad and high activity against Gram-negative pathogens, that can be enhanced in presence of citric and malic acid, and be used in human and veterinary medicine.Project “BioHealth – Biotechnology and Bioengineering approaches to improve health quality,” Ref. NORTE-07-0124-FEDER-000027, co-funded by the Programa Operacional Regional do Norte (ON.2 – O Novo Norte), QREN, FEDER. The authors also acknowledge the project “Consolidating Research Expertise and Resources on Cellular and Molecular Biotechnology at CEB/IBB,” Ref. FCOMP-01-0124-FEDER-027462 and the bilateral project CNR/FCT. Mass spectrometry analyses were carried out at the Faculty of Science Mass Spectrometry Centre, University of SheffieldFrontiers MediaUniversidade do MinhoOliveira, Hugo Alexandre MendesBoas, Diana Patrícia Andrade VilasMesnage, StéphaneKluskens, LeonLavigne, RobSillankorva, SannaSecundo, FrancescoAzeredo, Joana2016-022016-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/41411engOliveira, Hugo; Vilas Boas, Diana; Mesnage, Stéphane; Kluskens, Leon; Lavigne, R.; Sillankorva, Sanna; Secundo, Francesco; Azeredo, Joana, Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity. Frontiers in Microbiology, 7(208), 1-9, 20161664-302X1664-302X10.3389/fmicb.2016.00208http://journal.frontiersin.org/article/10.3389/fmicb.2016.00208/fullinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-07-21T12:02:46Zoai:repositorium.sdum.uminho.pt:1822/41411Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:52:49.332001Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
title Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
spellingShingle Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
Oliveira, Hugo Alexandre Mendes
Acinetobacter baumannii
Phage endolysins
Mass spectrometry
Circular dichroism
Antibacterial activity
Ciências Agrárias::Biotecnologia Agrária e Alimentar
Science & Technology
title_short Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
title_full Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
title_fullStr Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
title_full_unstemmed Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
title_sort Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity
author Oliveira, Hugo Alexandre Mendes
author_facet Oliveira, Hugo Alexandre Mendes
Boas, Diana Patrícia Andrade Vilas
Mesnage, Stéphane
Kluskens, Leon
Lavigne, Rob
Sillankorva, Sanna
Secundo, Francesco
Azeredo, Joana
author_role author
author2 Boas, Diana Patrícia Andrade Vilas
Mesnage, Stéphane
Kluskens, Leon
Lavigne, Rob
Sillankorva, Sanna
Secundo, Francesco
Azeredo, Joana
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Oliveira, Hugo Alexandre Mendes
Boas, Diana Patrícia Andrade Vilas
Mesnage, Stéphane
Kluskens, Leon
Lavigne, Rob
Sillankorva, Sanna
Secundo, Francesco
Azeredo, Joana
dc.subject.por.fl_str_mv Acinetobacter baumannii
Phage endolysins
Mass spectrometry
Circular dichroism
Antibacterial activity
Ciências Agrárias::Biotecnologia Agrária e Alimentar
Science & Technology
topic Acinetobacter baumannii
Phage endolysins
Mass spectrometry
Circular dichroism
Antibacterial activity
Ciências Agrárias::Biotecnologia Agrária e Alimentar
Science & Technology
description The present study demonstrates the antibacterial potential of a phage endolysin against Gram-negative pathogens, particularly against multidrug resistant strains of Acinetobacter baumannii. We have cloned, heterologously expressed and characterized a novel endolysin (ABgp46) from Acinetobacter phage vb_AbaP_CEB1 and tested its antibacterial activity against several multidrug-resistant A. baumannii strains. LC-MS revealed that ABgp46 is an N-acetylmuramidase, that is also active over a broad pH range (4.0-10.0) and temperatures up to 50°C. Interestingly, ABgp46 has intrinsic and specific anti-A. baumannii activity, reducing multidrug resistant strains by up to 2 logs within 2 hours. By combining ABgp46 with several organic acids that act as outer membrane permeabilizing agents, it is possible to increase and broaden antibacterial activity to include other Gram-negative bacterial pathogens. In the presence of citric and malic acid, ABgp46 reduces A. baumannii below the detection limit (> 5 log) and more than 4 logs P. aeruginosa and Salmonella Typhimurium strains. Overall, this globular endolysin exhibits a broad and high activity against Gram-negative pathogens, that can be enhanced in presence of citric and malic acid, and be used in human and veterinary medicine.
publishDate 2016
dc.date.none.fl_str_mv 2016-02
2016-02-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/1822/41411
url http://hdl.handle.net/1822/41411
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Oliveira, Hugo; Vilas Boas, Diana; Mesnage, Stéphane; Kluskens, Leon; Lavigne, R.; Sillankorva, Sanna; Secundo, Francesco; Azeredo, Joana, Structural and enzymatic characterization of ABgp46, a novel phage endolysin with broad anti-Gram-negative bacterial activity. Frontiers in Microbiology, 7(208), 1-9, 2016
1664-302X
1664-302X
10.3389/fmicb.2016.00208
http://journal.frontiersin.org/article/10.3389/fmicb.2016.00208/full
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Frontiers Media
publisher.none.fl_str_mv Frontiers Media
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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