Análisis de la proteína de unión al receptor (RBP) del bacteriófago vb_saus_baqsau1 DE Staphylococcus aureus
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2022
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Ediciones Universidad Simón Bolívar
Facultad de Ciencias Básicas y Biomédicas
Facultad de Ciencias Básicas y Biomédicas
Resumen
S. aureus fue declarado en 2017 por la OMS (Organización Mundial de la Salud) como un patógeno de preocupación por su alta tasa de resistencia a los antibióticos como meticilina y vancomicina, además, por presentar factores de virulencia que hacen de este microrganismo una amenaza para los sistemas de salud a nivel mundial. En la última década, se renovado el estudio de los Bacteriófagos o virus bacterianos como alternativa para el control de esta problemática. Sin embargo, el uso de estos virus puede representar un riesgo mayor ya que están implicados en la transferencia horizontal de genes entre bacterias. Es por esto, que recientes estudios se han centrado en proteínas derivadas de éstos, como enzimas líticas o las proteínas de unión al receptor (RBP). Éstas últimas, se encargan del reconocimiento y adhesión del virus a la bacteria anfitriona a través del ácido teicoico de la pared bacteriana. Este trabajo tiene como objetivo el análisis estructural de la proteína RBP del bacteriófago vB_SauS_BaqSau1, resultados podrían contribuir al desarrollo de nuevas aplicaciones para la industria alimentaria, clínica y/o veterinaria.
S. aureus was declared in 2017 by the WHO (World Health Organization) as a pathogen of concern due to its high rate of resistance to antibiotics such as methicillin and vancomycin, as well as for presenting virulence factors that make this microorganism a threat to health systems worldwide. In the last decade, the study of Bacteriophages or bacterial viruses was renewed as an alternative to control this problem. However, the use of these viruses may represent a greater risk as they are involved in horizontal gene transfer between bacteria. For this reason, recent studies have focused on proteins derived from these, such as lytic enzymes or receptor binding proteins (RBPs). The latter are responsible for the recognition and adhesion of the virus to the host bacteria through the teichoic acid of the bacterial wall. The objective of this work is the structural analysis of the RBP protein of the bacteriophage vB_SauS_BaqSau1, the results could contribute to the development of new applications for the food, clinical and/or veterinary industry
S. aureus was declared in 2017 by the WHO (World Health Organization) as a pathogen of concern due to its high rate of resistance to antibiotics such as methicillin and vancomycin, as well as for presenting virulence factors that make this microorganism a threat to health systems worldwide. In the last decade, the study of Bacteriophages or bacterial viruses was renewed as an alternative to control this problem. However, the use of these viruses may represent a greater risk as they are involved in horizontal gene transfer between bacteria. For this reason, recent studies have focused on proteins derived from these, such as lytic enzymes or receptor binding proteins (RBPs). The latter are responsible for the recognition and adhesion of the virus to the host bacteria through the teichoic acid of the bacterial wall. The objective of this work is the structural analysis of the RBP protein of the bacteriophage vB_SauS_BaqSau1, the results could contribute to the development of new applications for the food, clinical and/or veterinary industry
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Bacteriófagos, Receptores de Bacteriófagos, Terapia con bacteriófagos, Factores de virulencia, Ácido teicoico, Bacteriophages, Bacteriophage receptors, Virulence factors, Teichoic acid
