Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis

Detalhes bibliográficos
Autor(a) principal: Catalão, Maria João
Data de Publicação: 2019
Outros Autores: Filipe, Sérgio R., Pimentel, Madalena
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://doi.org/10.3389/fmicb.2019.00190
Resumo: This work was funded by a Research Grant 2018 of the European Society of Clinical Microbiology and Infectious Diseases (ESCMID) and Fundacao para a Ciencia e Tecnologia (FCT), Lisbon, Portugal, through research grant PTDC/BIA-MIC/31233/2017 awarded to MC.
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spelling Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesisAntibiotic resistanceCell wallMycobacteriaMycobacteriophage lysis enzymesPeptidoglycanTuberculosisβ-lactamsMicrobiologyMicrobiology (medical)SDG 3 - Good Health and Well-beingThis work was funded by a Research Grant 2018 of the European Society of Clinical Microbiology and Infectious Diseases (ESCMID) and Fundacao para a Ciencia e Tecnologia (FCT), Lisbon, Portugal, through research grant PTDC/BIA-MIC/31233/2017 awarded to MC.Tuberculosis (TB), which is caused by Mycobacterium tuberculosis (Mtb), is one of the leading cause of death by an infectious diseases. The biosynthesis of the mycobacterial cell wall (CW) is an area of increasing research significance, as numerous antibiotics used to treat TB target biosynthesis pathways of essential CW components. The main feature of the mycobacterial cell envelope is an intricate structure, the mycolyl-arabinogalactan-peptidoglycan (mAGP) complex responsible for its innate resistance to many commonly used antibiotics and involved in virulence. A hallmark of mAGP is its unusual peptidoglycan (PG) layer, which has subtleties that play a key role in virulence by enabling pathogenic species to survive inside the host and resist antibiotic pressure. This dynamic and essential structure is not a target of currently used therapeutics as Mtb is considered naturally resistant to most β-lactam antibiotics due to a highly active β-lactamase (BlaC) that efficiently hydrolyses many β-lactam drugs to render them ineffective. The emergence of multidrug- and extensive drug-resistant strains to the available antibiotics has become a serious health threat, places an immense burden on health care systems, and poses particular therapeutic challenges. Therefore, it is crucial to explore additional Mtb vulnerabilities that can be used to combat TB. Remodeling PG enzymes that catalyze biosynthesis and recycling of the PG are essential to the viability of Mtb and are therefore attractive targets for novel antibiotics research. This article reviews PG as an alternative antibiotic target for TB treatment, how Mtb has developed resistance to currently available antibiotics directed to PG biosynthesis, and the potential of targeting this essential structure to tackle TB by attacking alternative enzymatic activities involved in Mtb PG modifications and metabolism.DCV - Departamento de Ciências da VidaUCIBIO - Applied Molecular Biosciences UnitInstituto de Tecnologia Química e Biológica António Xavier (ITQB)RUNCatalão, Maria JoãoFilipe, Sérgio R.Pimentel, Madalena2019-09-19T22:37:20Z2019-02-112019-02-11T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://doi.org/10.3389/fmicb.2019.00190eng1664-302XPURE: 13570721http://www.scopus.com/inward/record.url?scp=85065905919&partnerID=8YFLogxKhttps://doi.org/10.3389/fmicb.2019.00190info: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:RCAAP2024-03-11T04:36:26Zoai:run.unl.pt:10362/81794Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:36:08.624705Repositório 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 Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
title Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
spellingShingle Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
Catalão, Maria João
Antibiotic resistance
Cell wall
Mycobacteria
Mycobacteriophage lysis enzymes
Peptidoglycan
Tuberculosis
β-lactams
Microbiology
Microbiology (medical)
SDG 3 - Good Health and Well-being
title_short Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
title_full Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
title_fullStr Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
title_full_unstemmed Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
title_sort Revisiting anti-tuberculosis therapeutic strategies that target the peptidoglycan structure and synthesis
author Catalão, Maria João
author_facet Catalão, Maria João
Filipe, Sérgio R.
Pimentel, Madalena
author_role author
author2 Filipe, Sérgio R.
Pimentel, Madalena
author2_role author
author
dc.contributor.none.fl_str_mv DCV - Departamento de Ciências da Vida
UCIBIO - Applied Molecular Biosciences Unit
Instituto de Tecnologia Química e Biológica António Xavier (ITQB)
RUN
dc.contributor.author.fl_str_mv Catalão, Maria João
Filipe, Sérgio R.
Pimentel, Madalena
dc.subject.por.fl_str_mv Antibiotic resistance
Cell wall
Mycobacteria
Mycobacteriophage lysis enzymes
Peptidoglycan
Tuberculosis
β-lactams
Microbiology
Microbiology (medical)
SDG 3 - Good Health and Well-being
topic Antibiotic resistance
Cell wall
Mycobacteria
Mycobacteriophage lysis enzymes
Peptidoglycan
Tuberculosis
β-lactams
Microbiology
Microbiology (medical)
SDG 3 - Good Health and Well-being
description This work was funded by a Research Grant 2018 of the European Society of Clinical Microbiology and Infectious Diseases (ESCMID) and Fundacao para a Ciencia e Tecnologia (FCT), Lisbon, Portugal, through research grant PTDC/BIA-MIC/31233/2017 awarded to MC.
publishDate 2019
dc.date.none.fl_str_mv 2019-09-19T22:37:20Z
2019-02-11
2019-02-11T00:00:00Z
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 https://doi.org/10.3389/fmicb.2019.00190
url https://doi.org/10.3389/fmicb.2019.00190
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 1664-302X
PURE: 13570721
http://www.scopus.com/inward/record.url?scp=85065905919&partnerID=8YFLogxK
https://doi.org/10.3389/fmicb.2019.00190
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.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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