Abstract
Simple SummaryMycobacterium tuberculosis is a bacterium of great medical importance because it causes tuberculosis, a disease that affects millions of people worldwide. Two important features are related to this bacterium: its ability to infect and survive inside the host, minimizing the immune response, and the burden of clinical isolates that are highly resistant to antibiotics treatment. These two phenomena are directly affected by cell envelope proteins, such as proteins from the ATP-Binding Cassette (ABC transporters) superfamily. In this review, we have compiled information on all the M. tuberculosis ABC transporters described so far, both from a functional and structural point of view, and show their relevance for the bacillus and the potential targets for studies aiming to control the microorganism and structural features.Mycobacterium tuberculosis 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 M. tuberculosis, with particular focus on the diversity of their structural features and relevance in infection and drug resistance.
Highlights
M. tuberculosis is the agent responsible for tuberculosis, with about 10 million people infected in the world in 2018, of which 1.2 million died in 2019 [1]
We have subdivided them into section, we describe the components and full importers systems that were identified in section, we describe the components and full importers systems that were identified in tuberculosis, including their roles to keep thefor bacillus in full activity
There are other importers that are exclusive to the M. tuberculosis complex or just present in a few species, such as UgpABCE, which is conserved in M. kansasii and M. marinum; PstS1/PstC1/PstA1/PstB, conserved in M. yogonense, M. intracellulare, and M. terrae; and the transporters Rv0072/Rv0073 and Rv2563/Rv2564, present in M. florentinum, M. rhodesiae, M. kansasii, M. terrae, and M. fortuitum
Summary
M. tuberculosis is the agent responsible for tuberculosis, with about 10 million people infected in the world in 2018, of which 1.2 million died in 2019 [1]. Rv1747 and Rv0987/86, putative exporters, have a non-canonical domain architecture, with two cytoplasmic phosphorylated Fork-Head Associated (FHA) domains and two extracellular domains per TMD, respectively This mixing of functions and structural features across families highlights how surprising and captivating the components of the M. tuberculosis inner membrane are and how little it is known about them and the proteins that belong to the bacillus envelope. We highlight the fact that the number of transporters in M. tuberculosis must be much higher than described, since searches
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