Tripartite ATP-Independent Periplasmic (TRAP) Transporters and Tripartite Tricarboxylate Transporters (TTT): From Uptake to Pathogenicity
| Autor: | David J. Kelly, Matheus E. Bianconi, Gavin H. Thomas, Leonardo T. Rosa |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
carboxylic acids
0301 basic medicine Microbiology (medical) high-affinity 030106 microbiology Immunology lcsh:QR1-502 Review Microbiology Tricarboxylate DNA-binding protein lcsh:Microbiology Structure-Activity Relationship 03 medical and health sciences Adenosine Triphosphate Protein sequencing Bacterial Proteins periplasmic binding-proteins Gene Virulence Chemistry Mutagenesis Membrane Transport Proteins Biological Transport Transporter Periplasmic space Protein Subunits Infectious Diseases Biochemistry Multigene Family solute transport Periplasmic Binding Proteins ATP-Binding Cassette Transporters Protein Binding secondary transporter |
| Zdroj: | Frontiers in Cellular and Infection Microbiology, Vol 8 (2018) Frontiers in Cellular and Infection Microbiology |
| ISSN: | 2235-2988 1664-302X |
| DOI: | 10.3389/fcimb.2018.00033 |
| Popis: | The ability to efficiently scavenge nutrients in the host is essential for the viability of any pathogen. All catabolic pathways must begin with the transport of substrate from the environment through the cytoplasmic membrane, a role executed by membrane transporters. Although several classes of cytoplasmic membrane transporters are described, high-affinity uptake of substrates occurs through Solute Binding-Protein (SBP) dependent systems. Three families of SBP dependant transporters are known; the primary ATP-binding cassette (ABC) transporters, and the secondary Tripartite ATP-independent periplasmic (TRAP) transporters and Tripartite Tricarboxylate Transporters (TTT). Far less well understood than the ABC family, the TRAP transporters are found to be abundant among bacteria from marine environments, and the TTT transporters are the most abundant family of proteins in many species of β-proteobacteria. In this review, recent knowledge about these families is covered, with emphasis on their physiological and structural mechanisms, relating to several examples of relevant uptake systems in pathogenicity and colonization, using the SiaPQM sialic acid uptake system from Haemophilus influenzae and the TctCBA citrate uptake system of Salmonella typhimurium as the prototypes for the TRAP and TTT transporters, respectively. High-throughput analysis of SBPs has recently expanded considerably the range of putative substrates known for TRAP transporters, while the repertoire for the TTT family has yet to be fully explored but both types of systems most commonly transport carboxylates. Specialized spectroscopic techniques and site-directed mutagenesis have enriched our knowledge of the way TRAP binding proteins capture their substrate, while structural comparisons show conserved regions for substrate coordination in both families. Genomic and protein sequence analyses show TTT SBP genes are strikingly overrepresented in some bacteria, especially in the β-proteobacteria and some α-proteobacteria. The reasons for this are not clear but might be related to a role for these proteins in signaling rather than transport. |
| Databáze: | OpenAIRE |
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