New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology

Detalhes bibliográficos
Autor(a) principal: Mendonça, Jacinta
Data de Publicação: 2022
Outros Autores: Guedes, Carla, Silva, Carina, Sá, Sara, Oliveira, Marco, Accioly, Gustavo, Baylina, Pilar, Barata, Pedro, Pereira, Cláudia, Fernandes, Ruben
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.14/36866
Resumo: The production of extended‐spectrum β‐lactamases (ESBLs) is the main defense mechanism found in Gram negative bacteria. Among all the ESBLs, the CTX‐M enzymes appear as the most efficient in terms of dissemination in different epidemiological contexts. CTX‐M enzymes exhibit a striking plas-ticity, with a large number of allelic variants distributed in several sublineages, which can be associated with functional heterogeneity of clinical relevance. This observational analytical study provides an update of this family, currently with more than 200 variants described, from a phylogenetic, molecular, and structural point of view through homology in amino acid sequences. Our data, combined with described literature, provide phylogenetic and structural evidence of a new group. Thus, herein, we propose six groups among CTX‐M enzymes: the already stablished CTX‐M‐1, CTX‐M‐2, CTX‐M‐8, CTX‐M‐9, and CTX‐M‐25 clusters, as well as CTX‐M‐151 as the new cluster.
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spelling New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biologyCTX‐M β‐lactamasesCTX‐M‐151 new groupExtended‐spectrum β‐lactamases (ESBL)The production of extended‐spectrum β‐lactamases (ESBLs) is the main defense mechanism found in Gram negative bacteria. Among all the ESBLs, the CTX‐M enzymes appear as the most efficient in terms of dissemination in different epidemiological contexts. CTX‐M enzymes exhibit a striking plas-ticity, with a large number of allelic variants distributed in several sublineages, which can be associated with functional heterogeneity of clinical relevance. This observational analytical study provides an update of this family, currently with more than 200 variants described, from a phylogenetic, molecular, and structural point of view through homology in amino acid sequences. Our data, combined with described literature, provide phylogenetic and structural evidence of a new group. Thus, herein, we propose six groups among CTX‐M enzymes: the already stablished CTX‐M‐1, CTX‐M‐2, CTX‐M‐8, CTX‐M‐9, and CTX‐M‐25 clusters, as well as CTX‐M‐151 as the new cluster.Veritati - Repositório Institucional da Universidade Católica PortuguesaMendonça, JacintaGuedes, CarlaSilva, CarinaSá, SaraOliveira, MarcoAccioly, GustavoBaylina, PilarBarata, PedroPereira, CláudiaFernandes, Ruben2022-03-03T11:32:46Z2022-022022-02-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/36866eng2079-773710.3390/biology1102025685124403836PMC886921635205122info: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:RCAAP2024-01-16T01:43:12Zoai:repositorio.ucp.pt:10400.14/36866Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:29:58.418431Repositório 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 New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
title New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
spellingShingle New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
Mendonça, Jacinta
CTX‐M β‐lactamases
CTX‐M‐151 new group
Extended‐spectrum β‐lactamases (ESBL)
title_short New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
title_full New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
title_fullStr New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
title_full_unstemmed New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
title_sort New CTX‐M group conferring β‐lactam resistance: a compendium of phylogenetic insights from biochemical, molecular, and structural biology
author Mendonça, Jacinta
author_facet Mendonça, Jacinta
Guedes, Carla
Silva, Carina
Sá, Sara
Oliveira, Marco
Accioly, Gustavo
Baylina, Pilar
Barata, Pedro
Pereira, Cláudia
Fernandes, Ruben
author_role author
author2 Guedes, Carla
Silva, Carina
Sá, Sara
Oliveira, Marco
Accioly, Gustavo
Baylina, Pilar
Barata, Pedro
Pereira, Cláudia
Fernandes, Ruben
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Veritati - Repositório Institucional da Universidade Católica Portuguesa
dc.contributor.author.fl_str_mv Mendonça, Jacinta
Guedes, Carla
Silva, Carina
Sá, Sara
Oliveira, Marco
Accioly, Gustavo
Baylina, Pilar
Barata, Pedro
Pereira, Cláudia
Fernandes, Ruben
dc.subject.por.fl_str_mv CTX‐M β‐lactamases
CTX‐M‐151 new group
Extended‐spectrum β‐lactamases (ESBL)
topic CTX‐M β‐lactamases
CTX‐M‐151 new group
Extended‐spectrum β‐lactamases (ESBL)
description The production of extended‐spectrum β‐lactamases (ESBLs) is the main defense mechanism found in Gram negative bacteria. Among all the ESBLs, the CTX‐M enzymes appear as the most efficient in terms of dissemination in different epidemiological contexts. CTX‐M enzymes exhibit a striking plas-ticity, with a large number of allelic variants distributed in several sublineages, which can be associated with functional heterogeneity of clinical relevance. This observational analytical study provides an update of this family, currently with more than 200 variants described, from a phylogenetic, molecular, and structural point of view through homology in amino acid sequences. Our data, combined with described literature, provide phylogenetic and structural evidence of a new group. Thus, herein, we propose six groups among CTX‐M enzymes: the already stablished CTX‐M‐1, CTX‐M‐2, CTX‐M‐8, CTX‐M‐9, and CTX‐M‐25 clusters, as well as CTX‐M‐151 as the new cluster.
publishDate 2022
dc.date.none.fl_str_mv 2022-03-03T11:32:46Z
2022-02
2022-02-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
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status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.14/36866
url http://hdl.handle.net/10400.14/36866
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2079-7737
10.3390/biology11020256
85124403836
PMC8869216
35205122
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eu_rights_str_mv openAccess
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