Estudio de la prevalencia de ß-lactamasas de espectro extendido e integron clase 1 en cepas obtenidas de hospitales de Mendoza y purificación de enzimas que participan en la síntesis del péptidoglicano de brucella para el diseño racional de inhibidores

Extended-spectrum β-lactamases (ESBLs) are a group diverse, complex and rapidly evolving enzymes that are posing a major therapeutic challenge today in the treatment of hospitalized. These enzymes share the ability to hydrolyze third-generation cephalosporins and aztreonam and yet are inhib...

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Autores principales: Buonfigli Carden, Julio Federico, Damiani, Armando Mario, García Castello, Miriam Concepción, Gatica Soria, Leonardo Martín, Marquez, Federico Adrián, Sanchez, Diego Germán
Publicado: 2019
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Acceso en línea:https://bdigital.uncu.edu.ar/fichas.php?idobjeto=14583
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Sumario:Extended-spectrum β-lactamases (ESBLs) are a group diverse, complex and rapidly evolving enzymes that are posing a major therapeutic challenge today in the treatment of hospitalized. These enzymes share the ability to hydrolyze third-generation cephalosporins and aztreonam and yet are inhibited by clavulanic acid. In addition, ESBL-producing organisms exhibit co-resistance to many other classes of antibiotics, resulting in limited therapeutic option.The dissemination of genes that impart resistance to antibiotics, especially those related to class 1 integrons, is a growing concern worldwide due to the substantial increase of strains resistant to multiple drugs. Resistance cassettes dissemination studies is an extremely relevant issue that concerns antibiotic administration policies. In this work, we determined the occurrence of class 1 integrons and extended-spectrum beta-lactamases in clinical isolates from local hospitals, using PCR techniques. Bacteria are capable of surviving the adverse conditions found at the hospital environment, and the use of antibiotic pressure turns them multi-resistant to various antimicrobials. Thus there is need for efficient infection-control practices for containment of outbreaks; and intervention strategies, e.g., antibiotic rotation to reduce further selection and spread of these increasingly resistant pathogens. On the other hand, the increase in the appearance of pathogenic bacterial strains with high resistance to antibiotic treatment constitutes a serious threat to public health. This situation has created an urgent need for the development of new antibacterial agents. One of the best-known and most validated targets for antibacterial therapy is the machinery for peptidoglycan (PG) biosynthesis. The PG is an essential component of the bacterial cell wall. In this project we propose, in collaboration with the group of Dr. Otero, the production, crystallization, and structure determination of the enzymes that synthesize PG en Brucella spp´s: PBP-1A, PBP-1B, PBP-2, -MurA, MurD, MurE and MurF, for rational design of antimicrobial drugs.