Phage-derived peptidoglycan degrading enzymes: challenges and future prospects for in vivo therapy
Autor(a) principal: | |
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Data de Publicação: | 2018 |
Outros Autores: | , |
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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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 |
repository.mail.fl_str_mv |
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1799132551810383872 |