المؤلفون: Forrellad, Marina Andrea, Blanco, Federico Carlos, Marrero Diaz de Villegas, Rubén, Vázquez, Cristina Lourdes, Yaneff, Agustín, García, Elizabeth Andrea, Gutierrez, Maximiliano Gabriel, Durán, Rosario, Villarino, Andrea, Bigi, Fabiana

المصدر: Frontiers in Microbiology; 10/22/2020, Vol. 11, pN.PAG-N.PAG, 14p

مصطلحات موضوعية: MYCOBACTERIUM tuberculosis, MYCOBACTERIUM smegmatis, SITE-specific mutagenesis, MITOGEN-activated protein kinase phosphatases, MYCOBACTERIA, LUNG diseases, ALKALINE phosphatase, AMINO acid residues

مستخلص: Tuberculosis, a lung disease caused by Mycobacterium tuberculosis (Mtb) , is one of the ten leading causes of death worldwide affecting mainly developing countries. Mtb can persist and survive inside infected cells through modulation of host antibacterial attack, i.e., by avoiding the maturation of phagosome containing mycobacteria to more acidic endosomal compartment. In addition, bacterial phosphatases play a central role in the interplay between host cells and Mtb. In this study, we characterized the Rv2577 of Mtb as a potential alkaline phosphatase/phosphodiesterase enzyme. By an in vitro kinetic assay, we demonstrated that purified Rv2577 expressed in Mycobacterium smegmatis displays both enzyme activities, as evidenced by using the artificial substrates p- NPP and bis-(p- NPP). In addition, a three-dimensional model of Rv2577 allowed us to define the catalytic amino acid residues of the active site, which were confirmed by site-directed mutagenesis and enzyme activity analysis, being characteristic of a member of the metallophosphatase superfamily. Finally, a mutation introduced in Rv2577 reduced the replication of Mtb in mouse organs and impaired the arrest of phagosomes containing mycobacteria in early endosomes; which indicates Rv2577 plays a role in Mtb virulence. [ABSTRACT FROM AUTHOR]

: Copyright of Frontiers in Microbiology is the property of Frontiers Media S.A. and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

المؤلفون: Forrellad, Marina Andrea, Blanco, Federico Carlos, Marrero Diaz de Villegas, Rubén, Vázquez, Cristina Lourdes, Yaneff, Agustín, Garcia, Elizabeth Andrea, Gutierrez, Maximiliano Gabriel, Durán, Rosario, Villarino, Andrea, Bigi, Fabiana

مصطلحات موضوعية: MYCOBACTERIUM TUBERCULOSIS, PHOSPHATASE, PHOSPHODIESTERASE, RV2577, VIRULENCE FACTOR, https://purl.org/becyt/ford/1.6Test, https://purl.org/becyt/ford/1Test

الوصف: Tuberculosis, a lung disease caused by Mycobacterium tuberculosis (Mtb), is one of the ten leading causes of death worldwide affecting mainly developing countries. Mtb can persist and survive inside infected cells through modulation of host antibacterial attack, i.e., by avoiding the maturation of phagosome containing mycobacteria to more acidic endosomal compartment. In addition, bacterial phosphatases play a central role in the interplay between host cells and Mtb. In this study, we characterized the Rv2577 of Mtb as a potential alkaline phosphatase/phosphodiesterase enzyme. By an in vitro kinetic assay, we demonstrated that purified Rv2577 expressed in Mycobacterium smegmatis displays both enzyme activities, as evidenced by using the artificial substrates p-NPP and bis-(p-NPP). In addition, a three-dimensional model of Rv2577 allowed us to define the catalytic amino acid residues of the active site, which were confirmed by site-directed mutagenesis and enzyme activity analysis, being characteristic of a member of the metallophosphatase superfamily. Finally, a mutation introduced in Rv2577 reduced the replication of Mtb in mouse organs and impaired the arrest of phagosomes containing mycobacteria in early endosomes; which indicates Rv2577 plays a role in Mtb virulence. ; Fil: Forrellad, Marina Andrea. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; Argentina ; Fil: Blanco, Federico Carlos. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación En Ciencias Veterinarias y Agronómicas. Instituto de Agrobiotecnología y Biología Molecular. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Agrobiotecnología y Biología Molecular; Argentina ...

وصف الملف: application/pdf

العلاقة: info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fmicb.2020.570794/fullTest; http://hdl.handle.net/11336/139063Test; Forrellad, Marina Andrea; Blanco, Federico Carlos; Marrero Diaz de Villegas, Rubén; Vázquez, Cristina Lourdes; Yaneff, Agustín; et al.; Rv2577 of Mycobacterium tuberculosis Is a Virulence Factor With Dual Phosphatase and Phosphodiesterase Functions; Frontiers Media S.A.; Frontiers in Microbiology; 11; 10-2020; 1-14; CONICET Digital; CONICET

الإتاحة: https://doi.org/10.3389/fmicb.2020.570794Test
http://hdl.handle.net/11336/139063Test