Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides

Tuberculosis, caused by <i>Mycobacterium tuberculosis</i>, is a lethal infectious disease of significant public health concern. The rise of multidrug-resistant and drug-tolerant strains has necessitated novel approaches to combat the disease. Toxin–antitoxin (TA) systems, key players in...

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Main Author: Sung-Min Kang
Format: Article
Language:English
Published: MDPI AG 2023-09-01
Series:Biomimetics
Subjects:
Online Access:https://www.mdpi.com/2313-7673/8/5/412
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author Sung-Min Kang
author_facet Sung-Min Kang
author_sort Sung-Min Kang
collection DOAJ
description Tuberculosis, caused by <i>Mycobacterium tuberculosis</i>, is a lethal infectious disease of significant public health concern. The rise of multidrug-resistant and drug-tolerant strains has necessitated novel approaches to combat the disease. Toxin–antitoxin (TA) systems, key players in bacterial adaptive responses, are prevalent in prokaryotic genomes and have been linked to tuberculosis. The genome of <i>M. tuberculosis</i> strains harbors an unusually high number of TA systems, prompting questions about their biological roles. The VapBC family, a representative type II TA system, is characterized by the VapC toxin, featuring a PilT N-terminal domain with nuclease activity. Its counterpart, VapB, functions as an antitoxin, inhibiting VapC’s activity. Additionally, we explore peptide mimics designed to replicate protein helical structures in this review. Investigating these synthetic peptides offers fresh insights into molecular interactions, potentially leading to therapeutic applications. These synthetic peptides show promise as versatile tools for modulating cellular processes and protein–protein interactions. We examine the rational design strategies employed to mimic helical motifs, their biophysical properties, and potential applications in drug development and bioengineering. This review aims to provide an in-depth understanding of TA systems by introducing known complex structures, with a focus on both structural aspects and functional and molecular details associated with each system.
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spelling doaj.art-a95a7ec4628f4665b7209cf08275dc3f2023-11-19T09:44:08ZengMDPI AGBiomimetics2313-76732023-09-018541210.3390/biomimetics8050412Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic PeptidesSung-Min Kang0College of Pharmacy, Duksung Women’s University, Seoul 01369, Republic of KoreaTuberculosis, caused by <i>Mycobacterium tuberculosis</i>, is a lethal infectious disease of significant public health concern. The rise of multidrug-resistant and drug-tolerant strains has necessitated novel approaches to combat the disease. Toxin–antitoxin (TA) systems, key players in bacterial adaptive responses, are prevalent in prokaryotic genomes and have been linked to tuberculosis. The genome of <i>M. tuberculosis</i> strains harbors an unusually high number of TA systems, prompting questions about their biological roles. The VapBC family, a representative type II TA system, is characterized by the VapC toxin, featuring a PilT N-terminal domain with nuclease activity. Its counterpart, VapB, functions as an antitoxin, inhibiting VapC’s activity. Additionally, we explore peptide mimics designed to replicate protein helical structures in this review. Investigating these synthetic peptides offers fresh insights into molecular interactions, potentially leading to therapeutic applications. These synthetic peptides show promise as versatile tools for modulating cellular processes and protein–protein interactions. We examine the rational design strategies employed to mimic helical motifs, their biophysical properties, and potential applications in drug development and bioengineering. This review aims to provide an in-depth understanding of TA systems by introducing known complex structures, with a focus on both structural aspects and functional and molecular details associated with each system.https://www.mdpi.com/2313-7673/8/5/412<i>Mycobacterium tuberculosis</i>toxin-antitoxin systemVapBC protein complex
spellingShingle Sung-Min Kang
Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
Biomimetics
<i>Mycobacterium tuberculosis</i>
toxin-antitoxin system
VapBC protein complex
title Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
title_full Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
title_fullStr Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
title_full_unstemmed Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
title_short Focused Overview of <i>Mycobacterium tuberculosis</i> VapBC Toxin–Antitoxin Systems Regarding Their Structural and Functional Aspects: Including Insights on Biomimetic Peptides
title_sort focused overview of i mycobacterium tuberculosis i vapbc toxin antitoxin systems regarding their structural and functional aspects including insights on biomimetic peptides
topic <i>Mycobacterium tuberculosis</i>
toxin-antitoxin system
VapBC protein complex
url https://www.mdpi.com/2313-7673/8/5/412
work_keys_str_mv AT sungminkang focusedoverviewofimycobacteriumtuberculosisivapbctoxinantitoxinsystemsregardingtheirstructuralandfunctionalaspectsincludinginsightsonbiomimeticpeptides