Novel In Silico Insights into Rv1417 and Rv2617c as Potential Protein Targets: The Importance of the Medium on the Structural Interactions with Exported Repetitive Protein (Erp) of Mycobacterium tuberculosis

Vista sencilla de ítem
dc.contributor.authorPaco-Chipana, Margot
dc.contributor.authorFebres-Molina, Camilo
dc.contributor.authorAguilar-Pineda, Jorge Alberto
dc.contributor.authorGómez, Badhin
dc.date.accessioned2023-10-23T01:57:39Z
dc.date.available2023-10-23T01:57:39Z
dc.date.issued2022-07-01
dc.descriptionINDEXACIÓN: SCOPUS.es
dc.description.abstractNowadays, tuberculosis is the second leading cause of death from a monopathogenic transmitted disease, only ahead of COVID-19. The role of exported repetitive protein (Erp) in the virulence of Mycobacterium tuberculosis has been extensively demonstrated. In vitro and in vivo assays have identified that Erp interacts with Rv1417 and Rv2617c proteins, forming putative transient molecular complexes prior to localization to the cell envelope. Although new insights into the interactions and functions of Erp have emerged over the years, knowledge about its structure and protein–protein interactions at the atomistic level has not been sufficiently explored. In this work, we have combined several in silico methodologies to gain new insights into the structural relationship between these proteins. Two system conditions were evaluated by MD simulations: Rv1417 and Rv2617c embedded in a lipid membrane and another with a semi-polar solvent to mimic the electrostatic conditions on the membrane surface. The Erp protein was simulated as an unanchored structure. Stabilized structures were docked, and complexes were evaluated to recognize the main residues involved in protein–protein interactions. Our results show the influence of the medium on the structural conformation of proteins. Globular conformations were favored under high polarity conditions and showed a higher energetic affinity in complex formation. Meanwhile, disordered conformations were favored under semi-polar conditions and an increase in the number of contacts between residues was observed. In addition, the electrostatic potential analysis showed remarkable changes in protein interactions due to the polarity of the medium, demonstrating the relevance of Erp protein in heterodimer formation. On the other hand, contact analysis showed that several C-terminal residues of Erp were involved in the protein interactions, which seems to contradict experimental observations; however, these complexes could be transient forms. The findings presented in this work are intended to open new perspectives in the studies of Erp protein molecular interactions and to improve the knowledge about its function and role in the virulence of Mycobacterium tuberculosis. © 2022 by the authors. Licensee MDPI, Basel, Switzerland.es
dc.identifier.citationPolymers, Volume 14, Issue 13, July-1 2022, Article number 2577es
dc.identifier.doi10.3390/polym14132577
dc.identifier.issn20734360
dc.identifier.urihttps://repositorio.unab.cl/xmlui/handle/ria/53531
dc.language.isoenes
dc.publisherMDPIes
dc.rights.licenseCC BY 4.0 DEED Attribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectErpes
dc.subjectmolecular dynamicses
dc.subjectRv1417es
dc.subjectRv2617ces
dc.subjecttuberculosises
dc.titleNovel In Silico Insights into Rv1417 and Rv2617c as Potential Protein Targets: The Importance of the Medium on the Structural Interactions with Exported Repetitive Protein (Erp) of Mycobacterium tuberculosises
dc.typeArtículoes
Archivos
Bloque original
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
polymers-14-02577-v2.pdf
Tamaño:
31.58 MB
Formato:
Adobe Portable Document Format
Descripción:
TEXTO COMPLETO EN INGLÉS.
Descargar
Bloque de licencias
Mostrando 1 - 1 de 1
No hay miniatura disponible
Nombre:
license.txt
Tamaño:
1.71 KB
Formato:
Item-specific license agreed upon to submission
Descripción:
Descargar
Colecciones
FCE - Artículos de Revista