Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy

Detalhes bibliográficos
Autor(a) principal: Oliveira, Hugo
Data de Publicação: 2018
Outros Autores: São-José, Carlos, 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/1822/55118
Resumo: Peptidoglycan degrading enzymes are of increasing interest as antibacterial agents, especially against multi-drug resistant pathogens. Herein we present a review about the biological features of virion-associated lysins and endolysins, phage-derived enzymes that have naturally evolved to compromise the bacterial peptidoglycan from without and from within, respectively. These natural features may determine the adaptability of the enzymes to kill bacteria in different environments. Endolysins are by far the most studied group of peptidoglycan-degrading enzymes, with several studies showing that they can exhibit potent antibacterial activity under specific conditions. However, the lytic activity of most endolysins seems to be significantly reduced when tested against actively growing bacteria, something that may be related to fact that these enzymes are naturally designed to degrade the peptidoglycan from within dead cells. This may negatively impact the efficacy of the endolysin in treating some infections in vivo. Here, we present a critical view of the methods commonly used to evaluate in vitro and in vivo the antibacterial performance of PG-degrading enzymes, focusing on the major hurdles concerning in vitro-to-in vivo translation.
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spelling Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapyBacteriophage-derived enzybioticsEndolysinIn vitroIn vivoVirion-associated lysinScience & TechnologyPeptidoglycan degrading enzymes are of increasing interest as antibacterial agents, especially against multi-drug resistant pathogens. Herein we present a review about the biological features of virion-associated lysins and endolysins, phage-derived enzymes that have naturally evolved to compromise the bacterial peptidoglycan from without and from within, respectively. These natural features may determine the adaptability of the enzymes to kill bacteria in different environments. Endolysins are by far the most studied group of peptidoglycan-degrading enzymes, with several studies showing that they can exhibit potent antibacterial activity under specific conditions. However, the lytic activity of most endolysins seems to be significantly reduced when tested against actively growing bacteria, something that may be related to fact that these enzymes are naturally designed to degrade the peptidoglycan from within dead cells. This may negatively impact the efficacy of the endolysin in treating some infections in vivo. Here, we present a critical view of the methods commonly used to evaluate in vitro and in vivo the antibacterial performance of PG-degrading enzymes, focusing on the major hurdles concerning in vitro-to-in vivo translation.By the Portuguese Foundation for Science and Technology (FCT) under the scope of the strategic funding of UID/BIO/04469/2013 unit, COMPETE 2020 (POCI-01-0145-FEDER-006684) and the Project PTDC/BBB-BSS/6471/2014 (POCI-01-0145-FEDER-016678). This work was also supported by BioTecNorte operation (NORTE-01-0145-FEDER-000004) funded by the European Regional Development Fund under the scope of Norte2020—Programa Operacional Regional do Norte. Hugo Oliveira acknowledges the FCT grant SFRH/BPD/111653/2015.info:eu-repo/semantics/publishedVersionMDPI AGUniversidade do MinhoOliveira, HugoSão-José, CarlosAzeredo, Joana20182018-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/55118engOliveira, Hugo; São-José, Carlos; Azeredo, Joana, Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy. Viruses, 10(6), 292, 20181999-49151999-491510.3390/v1006029229844287http://www.mdpi.com/journal/virusesinfo: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:RCAAP2023-07-21T12:19:01Zoai:repositorium.sdum.uminho.pt:1822/55118Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T19:11:52.518545Repositório 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 Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
title Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
spellingShingle Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
Oliveira, Hugo
Bacteriophage-derived enzybiotics
Endolysin
In vitro
In vivo
Virion-associated lysin
Science & Technology
title_short Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
title_full Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
title_fullStr Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
title_full_unstemmed Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
title_sort Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
author Oliveira, Hugo
author_facet Oliveira, Hugo
São-José, Carlos
Azeredo, Joana
author_role author
author2 São-José, Carlos
Azeredo, Joana
author2_role author
author
dc.contributor.none.fl_str_mv Universidade do Minho
dc.contributor.author.fl_str_mv Oliveira, Hugo
São-José, Carlos
Azeredo, Joana
dc.subject.por.fl_str_mv Bacteriophage-derived enzybiotics
Endolysin
In vitro
In vivo
Virion-associated lysin
Science & Technology
topic Bacteriophage-derived enzybiotics
Endolysin
In vitro
In vivo
Virion-associated lysin
Science & Technology
description Peptidoglycan degrading enzymes are of increasing interest as antibacterial agents, especially against multi-drug resistant pathogens. Herein we present a review about the biological features of virion-associated lysins and endolysins, phage-derived enzymes that have naturally evolved to compromise the bacterial peptidoglycan from without and from within, respectively. These natural features may determine the adaptability of the enzymes to kill bacteria in different environments. Endolysins are by far the most studied group of peptidoglycan-degrading enzymes, with several studies showing that they can exhibit potent antibacterial activity under specific conditions. However, the lytic activity of most endolysins seems to be significantly reduced when tested against actively growing bacteria, something that may be related to fact that these enzymes are naturally designed to degrade the peptidoglycan from within dead cells. This may negatively impact the efficacy of the endolysin in treating some infections in vivo. Here, we present a critical view of the methods commonly used to evaluate in vitro and in vivo the antibacterial performance of PG-degrading enzymes, focusing on the major hurdles concerning in vitro-to-in vivo translation.
publishDate 2018
dc.date.none.fl_str_mv 2018
2018-01-01T00:00:00Z
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/1822/55118
url http://hdl.handle.net/1822/55118
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv Oliveira, Hugo; São-José, Carlos; Azeredo, Joana, Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy. Viruses, 10(6), 292, 2018
1999-4915
1999-4915
10.3390/v10060292
29844287
http://www.mdpi.com/journal/viruses
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 MDPI AG
publisher.none.fl_str_mv MDPI AG
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
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