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Engineering acyl-homoserine lactone-interfering enzymes toward bacterial control.
Billot, Raphaël; Plener, Laure; Jacquet, Pauline; Elias, Mikael; Chabrière, Eric; Daudé, David.
Afiliação
  • Billot R; Gene&GreenTK, Marseille, France; IRD, APHM, MEPHI, IHU-Méditerranée Infection, Aix-Marseille Université, Marseille, France.
  • Plener L; Gene&GreenTK, Marseille, France.
  • Jacquet P; Gene&GreenTK, Marseille, France.
  • Elias M; Molecular Biology and Biophysics and Biotechnology Institute, Department of Biochemistry, University of Minnesota, St. Paul, Minnesota, USA.
  • Chabrière E; IRD, APHM, MEPHI, IHU-Méditerranée Infection, Aix-Marseille Université, Marseille, France. Electronic address: eric.chabriere@univ-amu.fr.
  • Daudé D; Gene&GreenTK, Marseille, France. Electronic address: david.daude@gene-greentk.com.
J Biol Chem ; 295(37): 12993-13007, 2020 09 11.
Article em En | MEDLINE | ID: mdl-32690609
ABSTRACT
Enzymes able to degrade or modify acyl-homoserine lactones (AHLs) have drawn considerable interest for their ability to interfere with the bacterial communication process referred to as quorum sensing. Many proteobacteria use AHL to coordinate virulence and biofilm formation in a cell density-dependent manner; thus, AHL-interfering enzymes constitute new promising antimicrobial candidates. Among these, lactonases and acylases have been particularly studied. These enzymes have been isolated from various bacterial, archaeal, or eukaryotic organisms and have been evaluated for their ability to control several pathogens. Engineering studies on these enzymes were carried out and successfully modulated their capacity to interact with specific AHL, increase their catalytic activity and stability, or enhance their biotechnological potential. In this review, special attention is paid to the screening, engineering, and applications of AHL-modifying enzymes. Prospects and future opportunities are also discussed with a view to developing potent candidates for bacterial control.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Hidrolases de Éster Carboxílico / Percepção de Quorum / Acil-Butirolactonas / Engenharia Metabólica / Antibacterianos Idioma: En Revista: J Biol Chem Ano de publicação: 2020 Tipo de documento: Article País de afiliação: França

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Bactérias / Proteínas de Bactérias / Hidrolases de Éster Carboxílico / Percepção de Quorum / Acil-Butirolactonas / Engenharia Metabólica / Antibacterianos Idioma: En Revista: J Biol Chem Ano de publicação: 2020 Tipo de documento: Article País de afiliação: França