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Gene Review

tonB1  -  protein TonB1

Pseudomonas aeruginosa PAO1

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Disease relevance of tonB


High impact information on tonB

  • This is a novel protein fold which appears to be preserved in all the periplasmic signalling domains of bacterial TonB-dependent outer membrane receptors that are involved in ECF signalling, because the hydrophobic residues that make up the core of the protein domain are highly conserved [3].
  • A low-iron milieu led to increased expression of the genes encoding TonB, alkaline protease,PrpL protease, exotoxin A, as well as fumarase C, Mn-dependent superoxide dismutase SodA, a ferredoxin and ferredoxin reductase and several oxidoreductases and dehydrogenases [6].
  • In vivo, the kinetics of formation of this FpvA-PaA-Fe complex are more than two orders of magnitude faster than in vitro and depend on the presence of TonB [7].
  • Unlike earlier studies with P. aeruginosa, we found that constitutive levels of gonococcal resistance to hydrophobic antimicrobial agents (i.e., Triton X-100 [TX-100]) did not require the TonB, ExbB, or ExbD protein [8].
  • The in vivo growth ability and lethal virulence were also restored by introduction of the tonB-carrying plasmid in the tonB mutant [1].

Chemical compound and disease context of tonB


Biological context of tonB

  • A tonB mutant of Pseudomonas aeruginosa deficient in iron siderophore uptake was shown in the present study to be hypersusceptible to a wide variety of antibiotics, reminiscent of the phenotype of mutants defective in the mexAB-oprM antibiotic efflux operon [9].
  • Thus, TonB plays an important role in both intrinsic and acquired antibiotic resistance in P. aeruginosa [9].
  • Targeting of the TonB1 fragment to the periplasm of P. aeruginosa inhibited the transport of ferric pyoverdine by FpvA in vivo, indicating an interference with endogenous TonB1, presumably caused by competition for binding sites at the transporter or by formation of nonfunctional TonB heterodimers [11].
  • The cytotoxin (31,700 Mr) lacks an N-terminal signal sequence for bacterial secretion but contains a pentapeptide consensus sequence commonly found in prokaryotic proteins which function in a TonB-dependent manner [12].
  • Neisserial TonB-dependent outer-membrane proteins: detection, regulation and distribution of three putative candidates identified from the genome sequences [13].

Associations of tonB with chemical compounds

  • These results indicate clearly that the intact tonB gene-and, therefore, the TonB protein encoded by it-is essential for iron acquisition mediated by pyoverdin and pyochelin and via heme uptake in P. aeruginosa and suggest that the TonB-dependent iron acquisition may be essential for P. aeruginosa to infect the animal host [1].

Other interactions of tonB


Analytical, diagnostic and therapeutic context of tonB

  • In addition, animal experiments showed that, in contrast to PAO1, the tonB mutant of PAO1 could not grow in vivo, such as in the muscles and lungs of immunosuppressed mice, and could not kill any of the animals [1].
  • TonB proteins are essential components in iron-siderophore uptake in bacteria, apparently functioning as energy transducers in coupling the energized state of the cytoplasmic membrane to outer-membrane receptor function [10].


  1. Requirement of the Pseudomonas aeruginosa tonB gene for high-affinity iron acquisition and infection. Takase, H., Nitanai, H., Hoshino, K., Otani, T. Infect. Immun. (2000) [Pubmed]
  2. Binding of iron-free siderophore, a common feature of siderophore outer membrane transporters of Escherichia coli and Pseudomonas aeruginosa. Hoegy, F., Celia, H., Mislin, G.L., Vincent, M., Gallay, J., Schalk, I.J. J. Biol. Chem. (2005) [Pubmed]
  3. Nuclear magnetic resonance solution structure of the periplasmic signalling domain of the TonB-dependent outer membrane transporter FecA from Escherichia coli. Garcia-Herrero, A., Vogel, H.J. Mol. Microbiol. (2005) [Pubmed]
  4. Haem utilization in Vibrio cholerae involves multiple TonB-dependent haem receptors. Mey, A.R., Payne, S.M. Mol. Microbiol. (2001) [Pubmed]
  5. The iron- and temperature-regulated cjrBC genes of Shigella and enteroinvasive Escherichia coli strains code for colicin Js uptake. Smajs, D., Weinstock, G.M. J. Bacteriol. (2001) [Pubmed]
  6. GeneChip expression analysis of the iron starvation response in Pseudomonas aeruginosa: identification of novel pyoverdine biosynthesis genes. Ochsner, U.A., Wilderman, P.J., Vasil, A.I., Vasil, M.L. Mol. Microbiol. (2002) [Pubmed]
  7. Iron-free pyoverdin binds to its outer membrane receptor FpvA in Pseudomonas aeruginosa: a new mechanism for membrane iron transport. Schalk, I.J., Hennard, C., Dugave, C., Poole, K., Abdallah, M.A., Pattus, F. Mol. Microbiol. (2001) [Pubmed]
  8. Inducible, but not constitutive, resistance of gonococci to hydrophobic agents due to the MtrC-MtrD-MtrE efflux pump requires TonB-ExbB-ExbD proteins. Rouquette-Loughlin, C., Stojiljkovic, I., Hrobowski, T., Balthazar, J.T., Shafer, W.M. Antimicrob. Agents Chemother. (2002) [Pubmed]
  9. Influence of the TonB energy-coupling protein on efflux-mediated multidrug resistance in Pseudomonas aeruginosa. Zhao, Q., Li, X.Z., Mistry, A., Srikumar, R., Zhang, L., Lomovskaya, O., Poole, K. Antimicrob. Agents Chemother. (1998) [Pubmed]
  10. The Pseudomonas aeruginosa tonB gene encodes a novel TonB protein. Poole, K., Zhao, Q., Neshat, S., Heinrichs, D.E., Dean, C.R. Microbiology (Reading, Engl.) (1996) [Pubmed]
  11. Interaction of TonB with the outer membrane receptor FpvA of Pseudomonas aeruginosa. Adams, H., Zeder-Lutz, G., Schalk, I., Pattus, F., Celia, H. J. Bacteriol. (2006) [Pubmed]
  12. The cytotoxin of Pseudomonas aeruginosa: cytotoxicity requires proteolytic activation. Orlik-Eisel, G., Lutz, F., Henschen, A., Eisel, U., Struckmeier, M., Kräuter, J., Niemann, H. Arch. Microbiol. (1990) [Pubmed]
  13. Neisserial TonB-dependent outer-membrane proteins: detection, regulation and distribution of three putative candidates identified from the genome sequences. Turner, P.C., Thomas, C.E., Stojiljkovic, I., Elkins, C., Kizel, G., Ala'Aldeen, D.A., Sparling, P.F. Microbiology (Reading, Engl.) (2001) [Pubmed]
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