Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes

Zhang, Lei; Li, Shuyu; Liu, Xiaozhen; Wang, Zhuo; Jiang, Mei; Wang, Ruiying; Xie, Laigong; Liu, Qinmeng; Xie, Xiaorong; Shang, Daohan; Li, Mengyun; Wei, Zhiyan; Wang, Yao; Fan, Chengpeng; Luo, Zhao‐Qing; Shen, Xihui

doi:10.1038/s41467-020-19243-5

Cited by 95 publications

(81 citation statements)

References 54 publications

(148 reference statements)

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“…The PctA chemoreceptor is a prime example of the complexity of bacterial signal transduction. Apart from binding amino acids [64] and GltB [71] , PctA also mediates chemotaxis to AI-2 [76] and histamine [63] . It has been shown that the PctA-LBD binds AI-2 directly with high affinity [76] , whereas it has been proposed that PctA mediates histamine chemotaxis through binding an unidentified SBP [63] .…”

Section: Gltb: a Sbp That Interacts With A Sensor Kinase And Chemoreceptorsmentioning

confidence: 99%

The role of solute binding proteins in signal transduction

Matilla

Ortega

Krell

2021

Computational and Structural Biotechnology Journal

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Section: Gltb: a Sbp That Interacts With A Sensor Kinase And Chemoreceptorsmentioning

confidence: 99%

The role of solute binding proteins in signal transduction

Matilla

Ortega

Krell

2021

Computational and Structural Biotechnology Journal

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“…Hydrophilic AI-2 is transported from the cell by the membrane protein TqsA [14]. Once a threshold concentration is reached in the late exponential phase, AI-2 is imported into E. coli through its recognition by the AI-2 receptor LsrB [15]. In addition to LsrB in E. coli, LuxP (e.g., Vibrio harveyi) and the dCACHE-domain proteins PctA/TlpQ (Pseudomonas aeruginosa) are receptors for AI-2 [15], so there are at least three forms of AI-2 receptors in different bacteria.…”

Section: Autoinducer-2mentioning

confidence: 99%

“…Once a threshold concentration is reached in the late exponential phase, AI-2 is imported into E. coli through its recognition by the AI-2 receptor LsrB [15]. In addition to LsrB in E. coli, LuxP (e.g., Vibrio harveyi) and the dCACHE-domain proteins PctA/TlpQ (Pseudomonas aeruginosa) are receptors for AI-2 [15], so there are at least three forms of AI-2 receptors in different bacteria. Furthermore, upon import, AI-2 is phosphorylated by LsrK in E. coli, and phosphorylated AI-2 binds and inhibits the repressor LsrR, which leads to changes in gene expression primarily at 37 °C [9].…”

Section: Autoinducer-2mentioning

confidence: 99%

The Primary Physiological Roles of Autoinducer 2 in Escherichia coli Are Chemotaxis and Biofilm Formation

Song

Wood

2021

Microorganisms

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Autoinducer 2 (AI-2) is a ubiquitous metabolite but, instead of acting as a “universal signal,” relatively few phenotypes have been associated with it, and many scientists believe AI-2 is often a metabolic byproduct rather than a signal. Here, the aim is to present evidence that AI-2 influences both biofilm formation and motility (swarming and chemotaxis), using Escherichia coli as the model system, to establish AI-2 as a true signal with an important physiological role in this bacterium. In addition, AI-2 signaling is compared to the other primary signal of E. coli, indole, and it is shown that they have opposite effects on biofilm formation and virulence.

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“…1A ) ( 14 ). Another family of receptors, of which each contains a pCACHE domain, was recently discovered, expanding AI-2 detection mechanisms and the breadth of bacterial species that apparently respond to AI-2 ( 15 ).…”

Section: Introductionmentioning

confidence: 99%

Saccharomyces cerevisiae Requires CFF1 To Produce 4-Hydroxy-5-Methylfuran-3(2H)-One, a Mimic of the Bacterial Quorum-Sensing Autoinducer AI-2

Valastyan

Kraml

Pelczer

et al. 2021

mBio

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Quorum sensing is a process of cell-to-cell communication that bacteria use to orchestrate collective behaviors. Quorum sensing depends on the production, release, and detection of extracellular signal molecules called autoinducers (AIs) that accumulate with increasing cell density. While most AIs are species specific, the AI called AI-2 is produced and detected by diverse bacterial species, and it mediates interspecies communication. We recently reported that mammalian cells produce an AI-2 mimic that can be detected by bacteria through the AI-2 receptor LuxP, potentially expanding the role of the AI-2 system to interdomain communication. Here, we describe a second molecule capable of interdomain signaling through LuxP, 4-hydroxy-5-methylfuran-3(2H)-one (MHF), that is produced by the yeast Saccharomyces cerevisiae. Screening the S. cerevisiae deletion collection revealed Cff1p, a protein with no known role, to be required for MHF production. Cff1p is proposed to be an enzyme, with structural similarity to sugar isomerases and epimerases, and substitution at the putative catalytic residue eliminated MHF production in S. cerevisiae. Sequence analysis uncovered Cff1p homologs in many species, primarily bacterial and fungal, but also viral, archaeal, and higher eukaryotic. Cff1p homologs from organisms from all domains can complement a cff1Δ S. cerevisiae mutant and restore MHF production. In all cases tested, the identified catalytic residue is conserved and required for MHF to be produced. These findings increase the scope of possibilities for interdomain interactions via AI-2 and AI-2 mimics, highlighting the breadth of molecules and organisms that could participate in quorum sensing. IMPORTANCE Quorum sensing is a cell-to-cell communication process that bacteria use to monitor local population density. Quorum sensing relies on extracellular signal molecules called autoinducers (AIs). One AI called AI-2 is broadly made by bacteria and used for interspecies communication. Here, we describe a eukaryotic AI-2 mimic, 4-hydroxy-5-methylfuran-3(2H)-one, (MHF), that is made by the yeast Saccharomyces cerevisiae, and we identify the Cff1p protein as essential for MHF production. Hundreds of viral, archaeal, bacterial, and eukaryotic organisms possess Cff1p homologs. This finding, combined with our results showing that homologs from all domains can replace S. cerevisiae Cff1p, suggests that like AI-2, MHF is widely produced. Our results expand the breadth of organisms that may participate in quorum-sensing-mediated interactions.

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Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes

Cited by 95 publications

References 54 publications

The role of solute binding proteins in signal transduction

The role of solute binding proteins in signal transduction

The Primary Physiological Roles of Autoinducer 2 in Escherichia coli Are Chemotaxis and Biofilm Formation

Saccharomyces cerevisiae Requires CFF1 To Produce 4-Hydroxy-5-Methylfuran-3(2H)-One, a Mimic of the Bacterial Quorum-Sensing Autoinducer AI-2

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