Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells?

Tuberculosis is an infectious disease caused by Mycobacterium tuberculosis (Mtb, i.e., the aetiological agent); the WHO has established this disease as high priority due to its ensuing mortality. Mtb uses a range of mechanisms for preventing its elimination by an infected host; new, viable alternatives for blocking the host-pathogen interaction are thus sought constantly. This article updates our laboratory's systematic search for antigens using bioinformatics tools to clarify the Mtb H37Rv Rv3632 protein's topology and location. This article reports a C-terminal region consisting of peptides 39255 and 39256 (81Thr-Arg114) having high specific binding regarding two infection-related cell lines (A549 and U937); they inhibited mycobacterial entry to U937 cells in a concentration-dependent manner. Rv3632 forms part of the mycobacterial cell envelope, formed by six linear synthetic peptides. Circular dichroism enabled determining the protein's secondary structure. It was also found that peptide 39254 (61Gly-Thr83) was a HABP for alveolar epithelial cells and inhibited mycobacteria entry to these cells regardless of concentration. Sera from active or latent tuberculosis patients did not recognise HABPs 39254 and 39256. These sequences represent a promising approach aiming at their ongoing modification and for including them when designing a multi-epitope, anti-tuberculosis vaccine. © 2019 Christian David Sánchez-Barinas et al.

• Fecha de publicación: 2019
• Institución: Universidad del Rosario
• Repositorio: Repositorio EdocUR - U. Rosario
• Idioma: eng
• OAI Identifier: oai:repository.urosario.edu.co:10336/23528
• Acceso en línea: https://doi.org/10.1155/2019/8680935; https://repository.urosario.edu.co/handle/10336/23528
• Palabra clave: Arginine; Epitope; Glycine; Peptide; Synthetic peptide; Threonine; Bacterial protein; Peptide; Protein binding; A-549 cell line; Animal cell; Article; Bacterial membrane; Bioinformatics; Carboxy terminal sequence; Circular dichroism; Concentration response; Female; Host pathogen interaction; Latent tuberculosis; Lung alveolus epithelium cell; Mortality; Mouse; Mycobacterium tuberculosis; Nonhuman; Protein secondary structure; Target cell; U-937 cell line; Amino acid sequence; Biology; Cell membrane; Cell wall; Chemistry; Genetic transcription; Genetics; Human; Isolation and purification; Metabolism; Molecular model; Mycobacterium tuberculosis; A549 cells; Amino acid sequence; Bacterial proteins; Cell membrane; Cell wall; Circular dichroism; Computational biology; Host-pathogen interactions; Humans; Mycobacterium tuberculosis; Peptides; Protein binding; U937 cells; genetic; secondary; molecular; Models; Protein structure; Transcription
• License: Abierto (Texto Completo)