The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics
<i>Mycobacterium tuberculosis</i> is the etiological agent of tuberculosis (TB), a disease that affects millions of people in the world and that is associated with several human diseases. The bacillus is highly adapted to infect and survive inside the host, mainly because of its cellular...
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| Format: | Article |
| Language: | English |
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MDPI AG
2020-12-01
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| Series: | Biology |
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| Online Access: | https://www.mdpi.com/2079-7737/9/12/443 |
| _version_ | 1797545756429647872 |
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| author | Marcelo Cassio Barreto de Oliveira Andrea Balan |
| author_facet | Marcelo Cassio Barreto de Oliveira Andrea Balan |
| author_sort | Marcelo Cassio Barreto de Oliveira |
| collection | DOAJ |
| description | <i>Mycobacterium tuberculosis</i> is the etiological agent of tuberculosis (TB), a disease that affects millions of people in the world and that is associated with several human diseases. The bacillus is highly adapted to infect and survive inside the host, mainly because of its cellular envelope plasticity, which can be modulated to adapt to an unfriendly host environment; to manipulate the host immune response; and to resist therapeutic treatment, increasing in this way the drug resistance of TB. The superfamily of ATP-Binding Cassette (ABC) transporters are integral membrane proteins that include both importers and exporters. Both types share a similar structural organization, yet only importers have a periplasmic substrate-binding domain, which is essential for substrate uptake and transport. ABC transporter-type importers play an important role in the bacillus physiology through the transport of several substrates that will interfere with nutrition, pathogenesis, and virulence. Equally relevant, exporters have been involved in cell detoxification, nutrient recycling, and antibiotics and drug efflux, largely affecting the survival and development of multiple drug-resistant strains. Here, we review known ABC transporters from <i>M. tuberculosis</i>, with particular focus on the diversity of their structural features and relevance in infection and drug resistance. |
| first_indexed | 2024-03-10T14:20:30Z |
| format | Article |
| id | doaj.art-6ee929d8054140ebbef2a406643b3244 |
| institution | Directory Open Access Journal |
| issn | 2079-7737 |
| language | English |
| last_indexed | 2024-03-10T14:20:30Z |
| publishDate | 2020-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biology |
| spelling | doaj.art-6ee929d8054140ebbef2a406643b32442023-11-20T23:27:00ZengMDPI AGBiology2079-77372020-12-0191244310.3390/biology9120443The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for TherapeuticsMarcelo Cassio Barreto de Oliveira0Andrea Balan1Laboratório de Biologia Estrutural Aplicada, Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo 05508000, BrazilLaboratório de Biologia Estrutural Aplicada, Department of Microbiology, Institute of Biomedical Sciences, University of São Paulo, São Paulo 05508000, Brazil<i>Mycobacterium tuberculosis</i> is the etiological agent of tuberculosis (TB), a disease that affects millions of people in the world and that is associated with several human diseases. The bacillus is highly adapted to infect and survive inside the host, mainly because of its cellular envelope plasticity, which can be modulated to adapt to an unfriendly host environment; to manipulate the host immune response; and to resist therapeutic treatment, increasing in this way the drug resistance of TB. The superfamily of ATP-Binding Cassette (ABC) transporters are integral membrane proteins that include both importers and exporters. Both types share a similar structural organization, yet only importers have a periplasmic substrate-binding domain, which is essential for substrate uptake and transport. ABC transporter-type importers play an important role in the bacillus physiology through the transport of several substrates that will interfere with nutrition, pathogenesis, and virulence. Equally relevant, exporters have been involved in cell detoxification, nutrient recycling, and antibiotics and drug efflux, largely affecting the survival and development of multiple drug-resistant strains. Here, we review known ABC transporters from <i>M. tuberculosis</i>, with particular focus on the diversity of their structural features and relevance in infection and drug resistance.https://www.mdpi.com/2079-7737/9/12/443<i>Mycobacterium tuberculosis</i>ABC transportersstructuredrug-effluximportersmce proteins |
| spellingShingle | Marcelo Cassio Barreto de Oliveira Andrea Balan The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics Biology <i>Mycobacterium tuberculosis</i> ABC transporters structure drug-efflux importers mce proteins |
| title | The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics |
| title_full | The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics |
| title_fullStr | The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics |
| title_full_unstemmed | The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics |
| title_short | The ATP-Binding Cassette (ABC) Transport Systems in <i>Mycobacterium tuberculosis</i>: Structure, Function, and Possible Targets for Therapeutics |
| title_sort | atp binding cassette abc transport systems in i mycobacterium tuberculosis i structure function and possible targets for therapeutics |
| topic | <i>Mycobacterium tuberculosis</i> ABC transporters structure drug-efflux importers mce proteins |
| url | https://www.mdpi.com/2079-7737/9/12/443 |
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