Thermothelomyces thermophilus exo- and endo-glucanases as tools for pathogenic E. coli biofilm degradation.

Autor: Samaniego LVB; Sao Carlos Institute of Physics, University of Sao Paulo, 1100 João Dagnone Avenue, São Carlos, SP, 13563-120, Brazil., Scandelau SL; Sao Carlos Institute of Physics, University of Sao Paulo, 1100 João Dagnone Avenue, São Carlos, SP, 13563-120, Brazil., Silva CR; Department of Biotechnology, Genetics and Cell Biology, State University of Maringá, Maringá, Brazil., Pratavieira S; Sao Carlos Institute of Physics, University of Sao Paulo, 1100 João Dagnone Avenue, São Carlos, SP, 13563-120, Brazil., de Oliveira Arnoldi Pellegrini V; Sao Carlos Institute of Physics, University of Sao Paulo, 1100 João Dagnone Avenue, São Carlos, SP, 13563-120, Brazil., Dabul ANG; Sao Carlos Institute of Physics, University of Sao Paulo, 1100 João Dagnone Avenue, São Carlos, SP, 13563-120, Brazil., Esmerino LA; Microbiology Laboratory, Clinical Analysis Department, Life Sciences and Health Institute, Ponta Grossa State University, Ponta Grossa, Brazil., de Oliveira Neto M; Institute of Biosciences, Sao Paulo State University, District of Rubiao Jr., Botucatu, SP, 18618-970, Brazil., Hernandes RT; Institute of Biosciences, Sao Paulo State University, District of Rubiao Jr., Botucatu, SP, 18618-970, Brazil., Segato F; Lorena School of Engineering, University of Sao Paulo, Estrada Municipal do Campinho, Lorena, SP, 12602-810, Brazil., Pileggi M; Environmental Microbiology Laboratory, Structural and Molecular Biology, and Genetics Department, Life Sciences and Health Institute, Ponta Grossa State University, Ponta Grossa, Brazil., Polikarpov I; Sao Carlos Institute of Physics, University of Sao Paulo, 1100 João Dagnone Avenue, São Carlos, SP, 13563-120, Brazil. ipolikarpov@ifsc.usp.br.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2024 Sep 29; Vol. 14 (1), pp. 22576. Date of Electronic Publication: 2024 Sep 29.
DOI: 10.1038/s41598-024-70144-9
Abstrakt: The escalating prevalence of drug-resistant pathogens not only jeopardizes the effectiveness of existing treatments but also increases the complexity and severity of infectious diseases. Escherichia coli is one the most common pathogens across all healthcare-associated infections. Enzymatic treatment of bacterial biofilms, targeting extracellular polymeric substances (EPS), can be used for EPS degradation and consequent increase in susceptibility of pathogenic bacteria to antibiotics. Here, we characterized three recombinant cellulases from Thermothelomyces thermophilus: a cellobiohydrolase I (TthCel7A), an endoglucanase (TthCel7B), and a cellobiohydrolase II (TthCel6A) as tools for hydrolysis of E. coli and Gluconacetobacter hansenii biofilms. Using a design mixture approach, we optimized the composition of cellulases, enhancing their synergistic activity to degrade the biofilms and significantly reducing the enzymatic dosage. In line with the crystalline and ordered structure of bacterial cellulose, the mixture of exo-glucanases (0.5 TthCel7A:0.5 TthCel6A) is effective in the hydrolysis of G. hansenii biofilm. Meanwhile, a mixture of exo- and endo-glucanases is required for the eradication of E. coli 042 and clinical E. coli biofilms with significantly different proportions of the enzymes (0.56 TthCel7B:0.44 TthCel6A and 0.6 TthCel7A:0.4 TthCel7B, respectively). X-ray diffraction pattern and crystallinity index of E. coli cellulose are comparable to those of carboxymethyl cellulose (CMC) substrate. Our results illustrate the complexity of E. coli biofilms and show that successful hydrolysis is achieved by a specific combination of cellulases, with consistent recurrence of TthCel7B endoglucanase.
(© 2024. The Author(s).)
Databáze: MEDLINE
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