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EcoSal Plus

Domain 9: Life in Communities and the Environment

Cell-to-Cell Signaling in and

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  • Authors: Melissa M. Kendall1, and Vanessa Sperandio2
  • Editor: James D. Kaper3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390; 2: Department of Microbiology, University of Texas Southwestern Medical Center, Dallas, TX 75390; 3: University of Maryland, School of Medicine, Baltimore, MD
  • Received 07 April 2009 Accepted 01 July 2009 Published 15 December 2009
  • Address correspondence to Vanessa Sperandio vanessa.sperandio@utsouthwestern.edu
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  • Abstract:

    Bacteria must be able to respond rapidly to changes in the environment in order to survive. One means of coordinating gene expression relies on tightly regulated and complex signaling systems. One of the first signaling systems that was described in detail is quorum sensing (QS). During QS, a bacterial cell produces and secretes a signaling molecule called an autoinducer (AI). As the density of the bacterial population increases, so does the concentration of secreted AI molecules, thereby allowing a bacterial species to coordinate gene expression based on population density. Subsequent studies have demonstrated that bacteria are also able to detect signal molecules produced by other species of bacteria as well as hormones produced by their mammalian hosts. These types of signaling interactions have been termed cell-to-cell signaling because the interaction does not rely on a threshold concentration of bacterial cells. This review discusses the three main types of cell-to-cell signaling mechanisms used by and , including the LuxR process, in which and detect signals produced by other species of bacteria; the LuxS/AI-2 system, in which and participate in intra- and interspecies signaling; and the AI-3/ epinephrine/norepinephrine system, in which and recognize self-produced AI, signal produced by other microbes, and/or the human stress hormones epinephrine or norepinephrine.

  • Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5

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Outer Membrane Proteins
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Cell-to-Cell Signaling in and

References

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2009-12-15
2017-05-24

Abstract:

Bacteria must be able to respond rapidly to changes in the environment in order to survive. One means of coordinating gene expression relies on tightly regulated and complex signaling systems. One of the first signaling systems that was described in detail is quorum sensing (QS). During QS, a bacterial cell produces and secretes a signaling molecule called an autoinducer (AI). As the density of the bacterial population increases, so does the concentration of secreted AI molecules, thereby allowing a bacterial species to coordinate gene expression based on population density. Subsequent studies have demonstrated that bacteria are also able to detect signal molecules produced by other species of bacteria as well as hormones produced by their mammalian hosts. These types of signaling interactions have been termed cell-to-cell signaling because the interaction does not rely on a threshold concentration of bacterial cells. This review discusses the three main types of cell-to-cell signaling mechanisms used by and , including the LuxR process, in which and detect signals produced by other species of bacteria; the LuxS/AI-2 system, in which and participate in intra- and interspecies signaling; and the AI-3/ epinephrine/norepinephrine system, in which and recognize self-produced AI, signal produced by other microbes, and/or the human stress hormones epinephrine or norepinephrine.

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Figures

Image of Figure 1
Figure 1

LuxI synthesizes AI-1 and diffuses outside the cell. When cell density and, therefore, AI-1 concentration, is high, AI-1 diffuses back into the cell where it binds to LuxR. LuxR complexed with AI-1 subsequently activates transcription of itself as well as the luciferase operon. IM, inner membrane; OM, outer membrane.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Image of Figure 2
Figure 2

(A) AI-1 is composed of a homoserine lactone ring bound to a fatty acid side chain. (B) SdiA detects oxoC8 and oxoC6 with greatest sensitivities. (C) SdiA can also detect other forms of AI-1, such as C8 and C6, although with less sensitivity.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 3

Once EHEC enters the rumen, it encounters AHLs. In the presence of AHLs, SdiA is functionally stable and acts to increase expression of acid tolerance genes in the operon and represses expression of the LEE genes. Upregulation of the genes allows EHEC to survive passage through the acidic abomasum. AHLs have not been detected in the colon; thus, SdiA is unstable, and EHEC can activate the LEE and colonize the renal anal junction of the colon.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 4

The and the genes encoded in this operon affect the transcription and folding, respectively, of plasmid-encoded fimbriae that are encoded by the upstream genes. SrgA plays a role in protein folding in the -encoded fimbriae by catalyzing disulfide bond formation ( 37 , 38 ).

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Image of Figure 5
Figure 5

In the activated methyl cycle, SAM is converted ultimately to homocysteine and DPD. LuxS catalyzes the last step in the pathway, resulting in DPD. AI-2 is derived from the unstable compound DPD.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 6

(A) AI-2 produced by . is (2,4)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran-borate (-THMF borate). (B) AI-2 produced by serovar Typhimurium is (2,4)-2-methyl-2,3,3,4-tetrahydroxy-tetrahydrofuran (-THMF).

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 7

The genes are transcribed in an operon, whereas and are divergently transcribed. LsrB binds AI-2, which is then imported by the Lsr ABC transport system. Inside the cell, AI-2 is phosphorylated by LsrK and is thought to interact with LsrR, relieving the repression of the operon.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 8

(A) Methionine is important in the cell for production of the vital metabolic enzyme SAM (involved in the methylation of lipids, RNA, DNA, and protein), and de novo synthesis of methionine requires homocysteine. (B) The mutant cannot produce homocysteine through SRH hydrolysis; therefore, the oxaloacetate/-glutamate pathway must be used. Oxaloacetate, -glutamate, and the AspC and TyrB transaminases are used to produce aspartate, which then can proceed through a series of reactions that result in the synthesis of homocysteine. Exclusive use of this pathway may lead to altered metabolism and amino acid content in the mutant, leading to reduced AI-3 synthesis.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 9

The structure of AI-3 is not known but may resemble the aromatic compounds epinephrine and norepinephrine.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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Figure 10

AI-3, epinephrine, and norepinephrine bind the membrane receptor protein QseC, resulting in autophosphorylation. Subsequently, QseC phosphorylates its response regulator QseB, initiating a complex phosphorelay signaling cascade that results in expression of the flagellar biosynthesis and motility genes (), Shiga toxin (), the locus of enterocyte effacement (LEE), and a second two-component system, QseEF, that also promotes expression of the LEE.

Citation: Kendall M, Sperandio V. 2009. Cell-to-Cell Signaling in and , EcoSal Plus 2009; doi:10.1128/ecosalplus.5.5
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