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 alternati...
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Acceso en línea: | https://repository.urosario.edu.co/handle/10336/23528 https://doi.org/10.1155/2019/8680935 |
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ir-10336-235282022-05-02T12:37:14Z Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? Sánchez-Barinas, Christian David Tabares, Luisa Bermúdez, Maritza Patarroyo, Manuel Elkin Ocampo, Marisol Patarroyo, Manuel A. 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 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. 2019 2020-05-26T00:02:49Z info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 23146141 23146133 https://repository.urosario.edu.co/handle/10336/23528 https://doi.org/10.1155/2019/8680935 eng info:eu-repo/semantics/openAccess application/pdf Hindawi Limited instname:Universidad del Rosario |
institution |
EdocUR - Universidad del Rosario |
collection |
DSpace |
language |
Inglés (English) |
topic |
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 |
spellingShingle |
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 Sánchez-Barinas, Christian David Tabares, Luisa Bermúdez, Maritza Patarroyo, Manuel Elkin Ocampo, Marisol Patarroyo, Manuel A. Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? |
description |
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. |
format |
Artículo (Article) |
author |
Sánchez-Barinas, Christian David Tabares, Luisa Bermúdez, Maritza Patarroyo, Manuel Elkin Ocampo, Marisol Patarroyo, Manuel A. |
author_facet |
Sánchez-Barinas, Christian David Tabares, Luisa Bermúdez, Maritza Patarroyo, Manuel Elkin Ocampo, Marisol Patarroyo, Manuel A. |
author_sort |
Sánchez-Barinas, Christian David |
title |
Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? |
title_short |
Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? |
title_full |
Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? |
title_fullStr |
Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? |
title_full_unstemmed |
Specific Binding Peptides from Rv3632: A Strategy for Blocking Mycobacterium tuberculosis Entry to Target Cells? |
title_sort |
specific binding peptides from rv3632: a strategy for blocking mycobacterium tuberculosis entry to target cells? |
publisher |
Hindawi Limited |
publishDate |
2019 |
url |
https://repository.urosario.edu.co/handle/10336/23528 https://doi.org/10.1155/2019/8680935 |
_version_ |
1740172656825597952 |
score |
12,131701 |