Study of iron metabolism in the human pathogen Acinetobacter baumannii
Autor(a) principal: | |
---|---|
Data de Publicação: | 2023 |
Tipo de documento: | Dissertação |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10362/163219 |
Resumo: | "Acinetobacter baumannii is a multidrug resistant nosocomial pathogen, that is considered by World Health Organization as a priority for research and development of new antibiotics. Iron is essential in all living organisms, as it is part of cofactors in proteins involved in multiple fundamental cellular processes. Iron is associated with proteins in Fe-S clusters, heme or mono/di-iron proteins. A. baumannii species have a variety of mechanisms for iron acquisition from the host environment, including heme uptake systems, siderophore secretion or iron passive diffusion through outer membrane porins. Cofactors such as heme and Fe-S clusters are synthesized by A. baumannii through the protoporphyrin-dependent branch and the ISC system, respectively. In this work, we aimed to study a possible link between proteins involved in heme biosynthesis and Fe-S cluster biogenesis pathways as well as understand how heme-bind proteins can acquire heme. For that, we focused on the interaction of proteins involved in the synthesis of Fe-S and heme cofactors, as well as proteins that harbor these cofactors for proper functioning.(...)" |
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Study of iron metabolism in the human pathogen Acinetobacter baumanniiAcinetobacter baumanniiiron uptakeheme biosynthesisFe-S clustersDomínio/Área Científica::Ciências Naturais"Acinetobacter baumannii is a multidrug resistant nosocomial pathogen, that is considered by World Health Organization as a priority for research and development of new antibiotics. Iron is essential in all living organisms, as it is part of cofactors in proteins involved in multiple fundamental cellular processes. Iron is associated with proteins in Fe-S clusters, heme or mono/di-iron proteins. A. baumannii species have a variety of mechanisms for iron acquisition from the host environment, including heme uptake systems, siderophore secretion or iron passive diffusion through outer membrane porins. Cofactors such as heme and Fe-S clusters are synthesized by A. baumannii through the protoporphyrin-dependent branch and the ISC system, respectively. In this work, we aimed to study a possible link between proteins involved in heme biosynthesis and Fe-S cluster biogenesis pathways as well as understand how heme-bind proteins can acquire heme. For that, we focused on the interaction of proteins involved in the synthesis of Fe-S and heme cofactors, as well as proteins that harbor these cofactors for proper functioning.(...)"Beas, JordiSaraiva, LígiaRUNMoniz, Beatriz2023-12-052023-10-012026-10-31T00:00:00Z2023-12-05T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10362/163219TID:203518802enginfo:eu-repo/semantics/embargoedAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-03-11T05:46:21Zoai:run.unl.pt:10362/163219Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:59:19.131941Repositório 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 |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
title |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
spellingShingle |
Study of iron metabolism in the human pathogen Acinetobacter baumannii Moniz, Beatriz Acinetobacter baumannii iron uptake heme biosynthesis Fe-S clusters Domínio/Área Científica::Ciências Naturais |
title_short |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
title_full |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
title_fullStr |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
title_full_unstemmed |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
title_sort |
Study of iron metabolism in the human pathogen Acinetobacter baumannii |
author |
Moniz, Beatriz |
author_facet |
Moniz, Beatriz |
author_role |
author |
dc.contributor.none.fl_str_mv |
Beas, Jordi Saraiva, Lígia RUN |
dc.contributor.author.fl_str_mv |
Moniz, Beatriz |
dc.subject.por.fl_str_mv |
Acinetobacter baumannii iron uptake heme biosynthesis Fe-S clusters Domínio/Área Científica::Ciências Naturais |
topic |
Acinetobacter baumannii iron uptake heme biosynthesis Fe-S clusters Domínio/Área Científica::Ciências Naturais |
description |
"Acinetobacter baumannii is a multidrug resistant nosocomial pathogen, that is considered by World Health Organization as a priority for research and development of new antibiotics. Iron is essential in all living organisms, as it is part of cofactors in proteins involved in multiple fundamental cellular processes. Iron is associated with proteins in Fe-S clusters, heme or mono/di-iron proteins. A. baumannii species have a variety of mechanisms for iron acquisition from the host environment, including heme uptake systems, siderophore secretion or iron passive diffusion through outer membrane porins. Cofactors such as heme and Fe-S clusters are synthesized by A. baumannii through the protoporphyrin-dependent branch and the ISC system, respectively. In this work, we aimed to study a possible link between proteins involved in heme biosynthesis and Fe-S cluster biogenesis pathways as well as understand how heme-bind proteins can acquire heme. For that, we focused on the interaction of proteins involved in the synthesis of Fe-S and heme cofactors, as well as proteins that harbor these cofactors for proper functioning.(...)" |
publishDate |
2023 |
dc.date.none.fl_str_mv |
2023-12-05 2023-10-01 2023-12-05T00:00:00Z 2026-10-31T00:00:00Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10362/163219 TID:203518802 |
url |
http://hdl.handle.net/10362/163219 |
identifier_str_mv |
TID:203518802 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/embargoedAccess |
eu_rights_str_mv |
embargoedAccess |
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 |
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