This Review discusses inter-kingdom hormonal signalling between bacteria and mammals, and between bacteria and plants. Several bacterial signalling compounds alter mammalian and plant gene expression, and signalling transduction mechanisms. Here, the authors show how mammalian hormones serve as signalling molecules that alter bacterial gene expression.
The parallels between signalling through receptor kinases in mammals and prokaryotes are also discussed, as well as the role of hormone receptor functional analogues in eukaryotes and bacteria.
Bacteria use adrenaline and noradrenaline to regulate several processes, including virulence, and recent discoveries of bacterial functional analogues of adrenergic receptors have shed light on the adrenergic cross-signalling that occurs between microorganisms and their hosts.
Host stress signals are used as signalling molecules by microorganisms. In addition to adrenergic signalling, the authors also discuss recent data that show how other mammalian stress signals, such as dynorphin, are used as signalling molecules by bacterial cells to control virulence-gene expression.
Inter-kingdom signalling occurs through lipidic compounds that use intracellular mammalian and bacterial receptors. This Review also addresses how bacterial lipidic signalling molecules, such as acyl homoserine lactones, modulate mammalian cell signalling and the immune system.
Finally, the authors discuss evolutionary evidence that some metabolism pathways in eukaryotic cells have evolved through horizontal transfer from bacterial genes.
Microorganisms and their hosts communicate with each other through an array of hormonal signals. This cross-kingdom cell-to-cell signalling involves small molecules, such as hormones that are produced by eukaryotes and hormone-like chemicals that are produced by bacteria. Cell-to-cell signalling between bacteria, usually referred to as quorum sensing, was initially described as a means by which bacteria achieve signalling in microbial communities to coordinate gene expression within a population. Recent evidence shows, however, that quorum-sensing signalling is not restricted to bacterial cell-to-cell communication, but also allows communication between microorganisms and their hosts.
This is a preview of subscription content
Subscribe to Journal
Get full journal access for 1 year
only $8.25 per issue
All prices are NET prices.
VAT will be added later in the checkout.
Tax calculation will be finalised during checkout.
Get time limited or full article access on ReadCube.
All prices are NET prices.
Hooper, L. V. & Gordon, J. I. Commensal host–bacterial relationships in the gut. Science 292, 1115–1118 (2001). Excellent review of the microbial regulation of host intestinal immune defence.
Nealson, K. H., Platt, T. & Hastings, J. W. Cellular control of the synthesis and activity of the bacterial luminescent system. J. Bacteriol. 104, 313–322 (1970).
Fuqua, C., Winans, S. C. & Greenberg, E. P. Census and consensus in bacterial ecosystems: the LuxR–LuxI family of quorum-sensing transcriptional regulators. Annu. Rev. Microbiol. 50, 727–751 (1996).
Telford, G. et al. The Pseudomonas aeruginosa quorum-sensing signal molecule N-(3-oxododecanoyl)-L-homoserine lactone has immunomodulatory activity. Infect. Immun. 66, 36–42 (1998).
Sperandio, V., Torres, A. G., Jarvis, B., Nataro, J. P. & Kaper, J. B. Bacteria–host communication: the language of hormones. Proc. Natl Acad. Sci. USA 100, 8951–8956 (2003). First description of adrenaline and NA regulation of the T3SS, and of motility and cross-talk with bacterial QS molecules.
Molina, P. E. Endocrine Physiology (The McGraw Hill Companies, New York, 2006).
Moghal, N. & Sternberg, P. W. Multiple positive and negative regulators of signaling by the EGF-receptor. Curr. Opin. Cell Biol. 11, 190–196 (1999).
Gallio, M., Sturgill, G., Rather, P. & Kylsten, P. A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes. Proc. Natl Acad. Sci. USA 99, 12208–12213 (2002).
Stevenson, L. G. et al. Rhomboid protease AarA mediates quorum-sensing in Providencia stuartii by activating TatA of the twin-arginine translocase. Proc. Natl Acad. Sci. USA 104, 1003–1008 (2007).
Rather, P. N., Parojcic, M. M. & Paradise, M. R. An extracellular factor regulating expression of the chromosomal aminoglycoside 2′-N-acetyltransferase of Providencia stuartii. Antimicrob. Agents Chemother. 41, 1749–1754 (1997).
Rather, P. N., Ding, X., Baca-DeLancey, R. R. & Siddiqui, S. Providencia stuartii genes activated by cell-to-cell signaling and identification of a gene required for production or activity of an extracellular factor. J. Bacteriol. 181, 7185–7191 (1999).
Lyte, M. The role of catecholamines in Gram-negative sepsis. Med. Hypotheses 37, 255–258 (1992). First description of NA-inducing bacterial growth.
Lyte, M. & Ernst, S. Catecholamine induced growth of Gram negative bacteria. Life Sci. 50, 203–212 (1992).
Lyte, M., Arulanandam, B. P. & Frank, C. D. Production of Shiga-like toxins by Escherichia coli O157:H7 can be influenced by the neuroendocrine hormone norepinephrine. J. Lab. Clin. Med. 128, 392–398 (1996).
Lyte, M. et al. Norepinephrine-induced expression of the K99 pilus adhesin of enterotoxigenic Escherichia coli. Biochem. Biophys. Res. Commun. 232, 682–686 (1997).
Freestone, P. P., Haigh, R. D., Williams, P. H. & Lyte, M. Involvement of enterobactin in norepinephrine-mediated iron supply from transferrin to enterohaemorrhagic Escherichia coli. FEMS Microbiol. Lett. 222, 39–43 (2003).
Freestone, P. P. et al. The mammalian neuroendocrine hormone norepinephrine supplies iron for bacterial growth in the presence of transferrin or lactoferrin. J. Bacteriol. 182, 6091–6098 (2000).
Burton, C. L. et al. The growth response of Escherichia coli to neurotransmitters and related catecholamine drugs requires a functional enterobactin biosynthesis and uptake system. Infect. Immun. 70, 5913–5923 (2002).
Clarke, M. B. & Sperandio, V. Transcriptional autoregulation by quorum sensing E. coli regulators B and C (QseBC) in enterohemorrhagic E. coli (EHEC). Mol. Microbiol. 58, 441–455 (2005).
Clarke, M. B. & Sperandio, V. Transcriptional regulation of flhDC by QseBC and σ28 (FliA) in enterohaemorrhagic Escherichia coli. Mol. Microbiol. 57, 1734–1749 (2005). First description of a bacterial adrenergic receptor.
Reading, N. C. et al. A novel two-component signaling system that activates transcription of an enterohemorrhagic Escherichia coli effector involved in remodeling of host actin. J. Bacteriol. 189, 2468–2476 (2007).
Kendall, M. M., Rasko, D. A. & Sperandio, V. Global effects of the cell-to-cell signaling molecules autoinducer-2, autoinducer-3, and epinephrine in a luxS mutant of enterohemorrhagic Escherichia coli. Infect. Immun. 75, 4875–4884 (2007).
Clarke, M. B., Hughes, D. T., Zhu, C., Boedeker, E. C. & Sperandio, V. The QseC sensor kinase: a bacterial adrenergic receptor. Proc. Natl Acad. Sci. USA 10420–10425 (2006).
Walters, M. & Sperandio, V. A Autoinducer 3 and epinephrine signaling in the kinetics of locus of enterocyte effacement gene expression in enterohemorrhagic Escherichia coli. Infect. Immun. 74, 5445–5455 (2006).
Walters, M., Sircili, M. P. & Sperandio, V. AI-3 synthesis is not dependent on luxS in Escherichia coli. J. Bacteriol. 188, 5668–5681 (2006).
Nakano, M., Takahashi, A., Sakai, Y. & Nakaya, Y. Modulation of pathogenicity with norepinephrine related to the type III secretion system of Vibrio parahaemolyticus. J. Infect. Dis. 195, 1353–1360 (2007).
Furness, J. B. Types of neurons in the enteric nervous system. J. Auton. Nerv. Syst. 81, 87–96 (2000).
Purves, D. et al. Neuroscience (Sinauer Associates, New York, 2001).
Horger, S., Schultheiss, G. & Diener, M. Segment-specific effects of epinephrine on ion transport in the colon of the rat. Am. J. Physiol. 275, G1367–G1376 (1998).
Freddolino, P. L. et al. Predicted 3D structure for the human β2 adrenergic receptor and its binding site for agonists and antagonists. Proc. Natl Acad. Sci. USA 101, 2736–2741 (2004).
Eldrup, E. & Richter, E. A. DOPA, dopamine, and DOPAC concentrations in the rat gastrointestinal tract decrease during fasting. Am. J. Physiol. Endocrinol. Metab. 279, E815–E822 (2000).
Kinney, K. S., Austin, C. E., Morton, D. S. & Sonnenfeld, G. Norepinephrine as a growth stimulating factor in bacteria — mechanistic studies. Life Sci. 67, 3075–3085 (2000).
Lamont, I. L., Beare, P. A., Ochsner, U., Vasil, A. I. & Vasil, M. L. Siderophore-mediated signaling regulates virulence factor production in Pseudomonas aeruginosa. Proc. Natl Acad. Sci. USA 99, 7072–7077 (2002).
Alverdy, J. et al. Gut-derived sepsis occurs when the right pathogen with the right virulence genes meets the right host: evidence for in vivo virulence expression in Pseudomonas aeruginosa. Ann. Surg. 232, 480–489 (2000).
Kaper, J. B. & O'Brien, A. D. Escherichia coli O157:H7 and other Shiga toxin-producing E. coli strains (ASM, Washington DC, 1998).
Moon, H. W., Whipp, S. C., Argenzio, R. A., Levine, M. M. & Giannella, R. A. Attaching and effacing activities of rabbit and human enteropathogenic Escherichia coli in pig and rabbit intestines. Infect. Immun. 41, 1340–1351 (1983).
Knutton, S., Baldini, M. M., Kaper, J. B. & McNeish, A. S. Role of plasmid-encoded adherence factors in adhesion of enteropathogenic Escherichia coli to HEp-2 cells. Infect. Immun. 55, 78–85 (1987).
Tzipori, S. et al. The pathogenesis of hemorrhagic colitis caused by Escherichia coli O157:H7 in gnotobiotic piglets. J. Infect. Dis. 154, 712–716 (1986).
McDaniel, T. K., Jarvis, K. G., Donnenberg, M. S. & Kaper, J. B. A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens. Proc. Natl Acad. Sci. USA 92, 1664–1668 (1995).
Jarvis, K. G. et al. Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation. Proc. Natl Acad. Sci. USA 92, 7996–8000 (1995).
Jerse, A. E., Yu, J., Tall, B. D. & Kaper, J. B. A genetic locus of enteropathogenic Escherichia coli necessary for the production of attaching and effacing lesions on tissue culture cells. Proc. Natl Acad. Sci. USA 87, 7839–7843 (1990).
Kenny, B. et al. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91, 511–520 (1997).
McNamara, B. P. & Donnenberg, M. S. A novel proline-rich protein, EspF, is secreted from enteropathogenic Escherichia coli via the type III export pathway. FEMS Microbiol. Lett. 166, 71–78 (1998).
Kenny, B. & Jepson, M. Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria. Cell. Microbiol. 2, 579–590 (2000).
Elliott, S. J. et al. EspG, a novel type III system-secreted protein from enteropathogenic Escherichia coli with similarities to VirA of Shigella flexneri. Infect. Immun. 69, 4027–4033 (2001).
Tu, X., Nisan, I., Yona, C., Hanski, E. & Rosenshine, I. EspH, a new cytoskeleton-modulating effector of enterohaemorrhagic and enteropathogenic Escherichia coli. Mol. Microbiol. 47, 595–606 (2003).
Kanack, K. J., Crawford, J. A., Tatsuno, I., Karmali, M. A. & Kaper, J. B. SepZ/EspZ is secreted and translocated into HeLa cells by the enteropathogenic Escherichia coli type III secretion system. Infect. Immun. 73, 4327–4337 (2005).
Karmali, M. A., Petric, M., Lim, C., Fleming, P. C. & Steele, B. T. Escherichia coli cytotoxin, haemolytic-uraemic syndrome, and haemorrhagic colitis. Lancet 2, 1299–1300 (1983).
Tannock, G. W. et al. Ecological behavior of Lactobacillus reuteri 100-23 is affected by mutation of the luxS gene. Appl. Environ. Microbiol. 71, 8419–8425 (2005).
Vlisidou, I. et al. The neuroendocrine stress hormone norepinephrine augments Escherichia coli O157:H7-induced enteritis and adherence in a bovine ligated ileal loop model of infection. Infect. Immun. 72, 5446–5451 (2004).
Sperandio, V., Torres, A. G., Giron, J. A. & Kaper, J. B. Quorum sensing is a global regulatory mechanism in enterohemorrhagic Escherichia coli O157:H7. J. Bacteriol. 183, 5187–5197 (2001).
Igo, M. M., Ninfa, A. J., Stock, J. B. & Silhavy, T. J. Phosphorylation and dephosphorylation of a bacterial transcriptional activator by a transmembrane receptor. Genes Dev. 3, 1725–1734 (1989).
Lyon, G. J. & Muir, T. W. Chemical signaling among bacteria and its inhibition. Chem. Biol. 10, 1007–1021 (2003).
Roychoudhury, S. et al. Inhibitors of two-component signal transduction systems: inhibition of alginate gene activation in Pseudomonas aeruginosa. Proc. Natl Acad. Sci. USA 90, 965–969 (1993).
Merighi, M., Carroll-Portillo, A., Septer, A. N., Bhatiya, A. & Gunn, J. S. Role of Salmonella enterica serovar Typhimurium two-component system PreA/PreB in modulating PmrA-regulated gene transcription. J. Bacteriol. 188, 141–149 (2006).
Bearson, B. L. & Bearson, S. M. The role of the QseC quorum-sensing sensor kinase in colonization and norepinephrine-enhanced motility of Salmonella enterica serovar Typhimurium. Microb. Pathog. 12 Oct 2007 (doi:10.1016/j.micpath.2007.10.001).
Callaway, T. R. et al. Social stress increases fecal shedding of Salmonella typhimurium by early weaned piglets. Curr. Issues Intest. Microbiol. 7, 65–71 (2006).
Weiss, D. S. et al. In vivo negative selection screen identifies genes required for Francisella virulence. Proc. Natl Acad. Sci. USA 104, 6037–6042 (2007).
Scheckelhoff, M. R., Telford, S. R., Wesley, M. & Hu, L. T. Borrelia burgdorferi intercepts host hormonal signals to regulate expression of outer surface protein A. Proc. Natl Acad. Sci. USA 104, 7247–7252 (2007).
Valet, P. et al. Characterization and distribution of α2-adrenergic receptors in the human intestinal mucosa. J. Clin. Invest. 91, 2049–2057 (1993).
Remaury, A., Larrouy, D., Daviaud, D., Rouot, B. & Paris, H. Coupling of the α2-adrenergic receptor to the inhibitory G-protein Gi and adenylate cyclase in HT29 cells. Biochem. J. 292, 283–288 (1993).
Buchman, A. L. et al. Clonidine reduces diarrhea and sodium loss in patients with proximal jejunostomy: a controlled study. J. Parenter. Enteral. Nutr. 30, 487–491 (2006).
Zaborina, O. et al. Dynorphin activates quorum sensing quinolone signaling in Pseudomonas aeruginosa. PLoS Pathog. 3, e35 (2007). First report of the dynorphin regulation of bacterial pathogenesis and cross-signalling with QS.
Reading, N. C. & Sperandio, V. Quorum sensing: the many languages of bacteria. FEMS Microbiol. Lett. 254, 1–11 (2006).
Yoon, S. S. et al. Pseudomonas aeruginosa anaerobic respiration in biofilms: relationships to cystic fibrosis pathogenesis. Dev. Cell 3, 593–603 (2002).
Singh, P. K. et al. Quorum-sensing signals indicate that cystic fibrosis lungs are infected with bacterial biofilms. Nature 407, 762–764 (2000).
Downward, J. The ins and outs of signalling. Nature 411, 759–762 (2001).
Shiner, E. K., Rumbaugh, K. P. & Williams, S. C. Inter-kingdom signaling: deciphering the language of acyl homoserine lactones. FEMS Microbiol. Rev. 29, 935–947 (2005).
Williams, S. C. et al. Pseudomonas aeruginosa autoinducer enters and functions in mammalian cells. J. Bacteriol. 186, 2281–2287 (2004).
DiMango, E., Zar, H. J., Bryan, R. & Prince, A. Diverse Pseudomonas aeruginosa gene products stimulate respiratory epithelial cells to produce interleukin-8. J. Clin. Invest. 96, 2204–2210 (1995).
Chhabra, S. R. et al. Synthetic analogues of the bacterial signal (quorum sensing) molecule N-(3-oxododecanoyl)-L-homoserine lactone as immune modulators. J. Med. Chem. 46, 97–104 (2003).
Ritchie, A. J., Yam, A. O., Tanabe, K. M., Rice, S. A. & Cooley, M. A. Modification of in vivo and in vitro T- and B-cell-mediated immune responses by the Pseudomonas aeruginosa quorum-sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone. Infect. Immun. 71, 4421–4431 (2003).
Ritchie, A. J. et al. The Pseudomonas aeruginosa quorum-sensing molecule N-3-(oxododecanoyl)-L-homoserine lactone inhibits T-cell differentiation and cytokine production by a mechanism involving an early step in T-cell activation. Infect. Immun. 73, 1648–1655 (2005).
Pritchard, D. I. et al. Alleviation of insulitis and moderation of diabetes in NOD mice following treatment with a synthetic Pseudomonas aeruginosa signal molecule, N-(3-oxododecanoyl)-L-homoserine lactone. Acta Diabetol. 42, 119–122 (2005).
Mota, L. J. & Cornelis, G. R. The bacterial injection kit: type III secretion systems. Ann. Med. 37, 234–249 (2005).
Tateda, K. et al. The Pseudomonas aeruginosa autoinducer N-3-oxododecanoyl homoserine lactone accelerates apoptosis in macrophages and neutrophils. Infect. Immun. 71, 5785–5793 (2003).
Horikawa, M. et al. Synthesis of Pseudomonas quorum-sensing autoinducer analogs and structural entities required for induction of apoptosis in macrophages. Bioorg. Med. Chem. Lett. 16, 2130–2133 (2006).
Shiner, E. K. et al. Pseudomonas aeruginosa autoinducer modulates host cell responses through calcium signalling. Cell. Microbiol. 8, 1601–1610 (2006).
Li, L., Hooi, D., Chhabra, S. R., Pritchard, D. & Shaw, P. E. Bacterial N-acylhomoserine lactone-induced apoptosis in breast carcinoma cells correlated with down-modulation of STAT3. Oncogene 23, 4894–4902 (2004).
Zimmermann, S. et al. Induction of neutrophil chemotaxis by the quorum-sensing molecule N-(3-oxododecanoyl)-L-homoserine lactone. Infect. Immun. 74, 5687–5692 (2006).
Smith, R. S. et al. IL-8 production in human lung fibroblasts and epithelial cells activated by the Pseudomonas autoinducer N-3-oxododecanoyl homoserine lactone is transcriptionally regulated by NF-κB and activator protein-2. J. Immunol. 167, 366–374 (2001).
Smith, R. S., Harris, S. G., Phipps, R. & Iglewski, B. The Pseudomonas aeruginosa quorum-sensing molecule N-(3-oxododecanoyl)homoserine lactone contributes to virulence and induces inflammation in vivo. J. Bacteriol. 184, 1132–1139 (2002).
Smith, R. S., Kelly, R., Iglewski, B. H. & Phipps, R. P. The Pseudomonas autoinducer N-(3-oxododecanoyl) homoserine lactone induces cyclooxygenase-2 and prostaglandin E2 production in human lung fibroblasts: implications for inflammation. J. Immunol. 169, 2636–2642 (2002).
Rumbaugh, K. P. Convergence of hormones and autoinducers at the host/pathogen interface. Anal. Bioanal. Chem. 387, 425–435 (2007).
Yang, F. et al. Quorum quenching enzyme activity is widely conserved in the sera of mammalian species. FEBS Lett. 579, 3713–3717 (2005).
Chun, C. K., Ozer, E. A., Welsh, M. J., Zabner, J. & Greenberg, E. P. Inactivation of a Pseudomonas aeruginosa quorum-sensing signal by human airway epithelia. Proc. Natl Acad. Sci. USA 101, 3587–3590 (2004). First report of mammalian cell inactivation of bacterial AHLs.
Khersonsky, O. & Tawfik, D. S. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 44, 6371–6382 (2005).
Draganov, D. I. et al. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 46, 1239–1247 (2005). First report that PONs are responsible for AHL inactivation.
Ozer, E. A. et al. Human and murine paraoxonase 1 are host modulators of Pseudomonas aeruginosa quorum-sensing. FEMS Microbiol. Lett. 253, 29–37 (2005).
Stoltz, D. A. et al. Paraoxonase-2 deficiency enhances Pseudomonas aeruginosa quorum sensing in murine tracheal epithelia. Am. J. Physiol. Lung Cell. Mol. Physiol. 292, L852–L860 (2007).
Zhang, R. G. et al. Structure of a bacterial quorum-sensing transcription factor complexed with pheromone and DNA. Nature 417, 971–974 (2002). First crystal structure of the bacterial AHL receptor TraR.
Vannini, A. et al. The crystal structure of the quorum sensing protein TraR bound to its autoinducer and target DNA. EMBO J. 21, 4393–4401 (2002).
Yao, Y. et al. Structure of the Escherichia coli quorum sensing protein SdiA: activation of the folding switch by acyl homoserine lactones. J. Mol. Biol. 355, 262–273 (2006).
Bottomley, M. J., Muraglia, E., Bazzo, R. & Carfi, A. Molecular insights into quorum sensing in the human pathogen Pseudomonas aeruginosa from the structure of the virulence regulator LasR bound to its autoinducer. J. Biol. Chem. 282, 13592–13600 (2007).
Ho, Y. S., Burden, L. M. & Hurley, J. H. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO J. 19, 5288–5299 (2000).
Harper, S. M., Neil, L. C. & Gardner, K. H. Structural basis of a phototropin light switch. Science 301, 1541–1544 (2003).
Gu, Y. Z., Hogenesch, J. B. & Bradfield, C. A. The PAS superfamily: sensors of environmental and developmental signals. Annu. Rev. Pharmacol. Toxicol. 40, 519–561 (2000).
Dioum, E. M. et al. NPAS2: a gas-responsive transcription factor. Science 298, 2385–2387 (2002).
Wu, L. et al. Recognition of host immune activation by Pseudomonas aeruginosa. Science 309, 774–777 (2005).
Bader, M. W. et al. Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 122, 461–472 (2005).
Bauer, W. D. & Mathesius, U. Plant responses to bacterial quorum sensing signals. Curr. Opin. Plant Biol. 7, 429–433 (2004).
Mathesius, U. et al. Extensive and specific responses of a eukaryote to bacterial quorum-sensing signals. Proc. Natl Acad. Sci. USA 100, 1444–1449 (2003). Extensive report of bacteria–plant cross-hormonal signalling.
Lugtenberg, B., Tikhonovich, I. & Provorov, N. (eds) Biology of Molecular Plant–Microbe Interactions Vol. 4 (IS-MPMI, Minnesota, 2004).
Manefield, M. et al. Halogenated furanones inhibit quorum sensing through accelerated LuxR turnover. Microbiology 148, 1119–1127 (2002).
Chevrot, R. et al. GABA controls the level of quorum-sensing signal in Agrobacterium tumefaciens. Proc. Natl Acad. Sci. USA 103, 7460–7464 (2006).
Keshavan, N. D., Chowdhary, P. K., Haines, D. C. & Gonzalez, J. E. L-Canavanine made by Medicago sativa interferes with quorum sensing in Sinorhizobium meliloti. J. Bacteriol. 187, 8427–8436 (2005).
Persson, T. et al. Rational design and synthesis of new quorum-sensing inhibitors derived from acylated homoserine lactones and natural products from garlic. Org. Biomol. Chem. 3, 253–262 (2005).
Perret, X., Staehelin, C. & Broughton, W. J. Molecular basis of symbiotic promiscuity. Microbiol. Mol. Biol. Rev. 64, 180–201 (2000).
Iyer, L. M., Aravind, L., Coon, S. L., Klein, D. C. & Koonin, E. V. Evolution of cell–cell signaling in animals: did late horizontal gene transfer from bacteria have a role? Trends Genet. 20, 292–299 (2004).
Coon, S. L. et al. Pineal serotonin N-acetyltransferase: expression cloning and molecular analysis. Science 270, 1681–1683 (1995).
Work in the laboratory of V.S. is supported by the National Institutes of Health, The Ellison Medical Foundation and Burroughs Wellcome Fund. The authors thank M. Lyte for comments on this manuscript. They also apologize to the numerous investigators whose manuscripts could not be cited owing to space constraints.
Entrez Genome Project
A bacterial hormone-like signalling molecule.
- Enteric nervous system
A nervous system that innervates the gastrointestinal tract.
A small organic molecule that is produced by bacteria to sequester iron.
- Type III secretion system
A specialized syringe-like secretion system that is used to inject bacterial effectors into host cells.
- Haemolytic uraemic syndrome
A complication, caused mostly by Shiga toxin, that can cause the kidneys to shut down and results in high morbidity and mortality.
An epithelial cell in the intestine.
- Eicosanoid family
A lipid-based signalling molecule that is best known for its control of the immune response. Prostaglandins are part of the eicosanoid family.
- T helper 1 (TH1) response
The actions of CD4 helper T lymphocytes can be summarized by two pathways, TH1 and TH2, on the basis of the cytokines that they produce and their effector functions. During the TH1 response, T helper lymphocytes principally secrete interferon-γ to activate phagocyte-mediated defence, which typically involves intracellular microorganisms.
- Paraoxonase family
A three-member gene family that consists of PON1, PON2 and PON3. Mammalian biological functions of paraoxonases remain elusive. However, possible functions include: protection from organophosphate poisoning; a protective role in vascular disease through lipoprotein lipid oxidation; and the limitation of bacterial infection through potential lactonase activity.
- PAS and GAF domain
A ubiquitous protein motif that is conserved in prokaryotes and eukaryotes.
About this article
Cite this article
Hughes, D., Sperandio, V. Inter-kingdom signalling: communication between bacteria and their hosts. Nat Rev Microbiol 6, 111–120 (2008). https://doi.org/10.1038/nrmicro1836
Antimicrobial resistance, virulence factors, and genotypes of Pseudomonas aeruginosa clinical isolates from Gorgan, northern Iran
International Microbiology (2022)
Archives of Microbiology (2022)
Veterinary Research (2021)
The Journal of Basic and Applied Zoology (2021)