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Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria

β-lactamases, which are found in several bacterial species and environments, are the main cause of resistance to β-lactams in Gram-negative bacteria. In 2009, a protein (LRA-13) with two β-lactamase domains (one class C domain and one class D domain) was experimentally characterised, and an extended...

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Autores principales: Silveira, Melise Chaves, Catanho, Marcos, de Miranda, Antônio Basílio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Instituto Oswaldo Cruz, Ministério da Saúde 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5967600/
https://www.ncbi.nlm.nih.gov/pubmed/29846396
http://dx.doi.org/10.1590/0074-02760180098
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author Silveira, Melise Chaves
Catanho, Marcos
de Miranda, Antônio Basílio
author_facet Silveira, Melise Chaves
Catanho, Marcos
de Miranda, Antônio Basílio
author_sort Silveira, Melise Chaves
collection PubMed
description β-lactamases, which are found in several bacterial species and environments, are the main cause of resistance to β-lactams in Gram-negative bacteria. In 2009, a protein (LRA-13) with two β-lactamase domains (one class C domain and one class D domain) was experimentally characterised, and an extended action spectrum against β-lactams consistent with two functional domains was found. Here, we present the results of searches in the non-redundant NCBI protein database that revealed the existence of a group of homologous bifunctional β-lactamases in the genomes of environmental bacteria. These findings suggest that bifunctional β-lactamases are widespread in nature; these findings also raise concern that bifunctional β-lactamases may be transferred to bacteria of clinical importance through lateral gene transfer mechanisms.
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spelling pubmed-59676002018-05-31 Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria Silveira, Melise Chaves Catanho, Marcos de Miranda, Antônio Basílio Mem Inst Oswaldo Cruz Short Communication β-lactamases, which are found in several bacterial species and environments, are the main cause of resistance to β-lactams in Gram-negative bacteria. In 2009, a protein (LRA-13) with two β-lactamase domains (one class C domain and one class D domain) was experimentally characterised, and an extended action spectrum against β-lactams consistent with two functional domains was found. Here, we present the results of searches in the non-redundant NCBI protein database that revealed the existence of a group of homologous bifunctional β-lactamases in the genomes of environmental bacteria. These findings suggest that bifunctional β-lactamases are widespread in nature; these findings also raise concern that bifunctional β-lactamases may be transferred to bacteria of clinical importance through lateral gene transfer mechanisms. Instituto Oswaldo Cruz, Ministério da Saúde 2018-05-28 /pmc/articles/PMC5967600/ /pubmed/29846396 http://dx.doi.org/10.1590/0074-02760180098 Text en https://creativecommons.org/licenses/by/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Short Communication
Silveira, Melise Chaves
Catanho, Marcos
de Miranda, Antônio Basílio
Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria
title Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria
title_full Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria
title_fullStr Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria
title_full_unstemmed Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria
title_short Genomic analysis of bifunctional Class C-Class D β-lactamases in environmental bacteria
title_sort genomic analysis of bifunctional class c-class d β-lactamases in environmental bacteria
topic Short Communication
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5967600/
https://www.ncbi.nlm.nih.gov/pubmed/29846396
http://dx.doi.org/10.1590/0074-02760180098
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