High-Affinity Chemotaxis to Histamine Mediated by the TlpQ Chemoreceptor of the Human Pathogen Pseudomonas aeruginosa

Corral-Lugo, Andrés; Matilla, Miguel A.; Martín‐Mora, David; Jiménez, Hortencia Silva; Torres, Noel; Kato, Junichi; Hida, Akiko; Oku, Shota; Conejero-Muriel, Mayte; Gavira, José A.; Krell, Tino

doi:10.1128/mbio.01894-18

Cited by 61 publications

(92 citation statements)

References 82 publications

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“…Sequence analysis indicates that both PctA and TlpQ harbor a ligand-binding domain (LBD) of the dCACHE family, a structure with two extracytoplasmic PAS-like subdomains termed membrane-proximal and membrane-distal modules, respectively 24 , 25 . Although PctA and TlpQ share only ~17% sequence identity in the LBD regions (Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Although PctA and TlpQ share only ~17% sequence identity in the LBD regions (Supplementary Fig. 1 ), alignment of the 3D structures of PctA-LBD (PDB ID: 5LTX) 26 and TlpQ-LBD (PDB ID: 6FU4) 24 using TM-align 27 suggests that they are mostly in the same fold (TM-score = 0.79, Supplementary Fig. 2 ).…”

Section: Resultsmentioning

confidence: 99%

“…Both PctA and TlpQ are known to drive chemotactic responses by directly binding to specific ligands 24 , 28 , 29 . Whereas PctA-LBD appears to exclusively bind amino acids 28 , 29 , TlpQ-LBD specifically recognizes histamine and polyamines 24 . Despite the well-established ligands for PctA-LBD and TlpQ-LBD, the results from chemotaxis tests (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…A pocket in the membrane-distal module of both PctA-LBD and TlpQ-LBD is involved in ligand recognition 24 , 26 , 28 . Calculation of the binding isotherm data showed that AI-2 binds to PctA-LBD and TlpQ-LBD in a 1:1 stoichiometry ( n = 0.93–1.29 sites) (Fig.…”

Section: Resultsmentioning

confidence: 99%

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Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes

et al. 2020

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Autoinducer-2 (AI-2) is a quorum sensing signal that mediates communication within and between many bacterial species. However, its known receptors (LuxP and LsrB families) are not found in all the bacteria capable of responding to this signaling molecule. Here, we identify a third type of AI-2 receptor, consisting of a dCACHE domain. AI-2 binds to the dCACHE domain of chemoreceptors PctA and TlpQ of Pseudomonas aeruginosa, thus inducing chemotaxis and biofilm formation. Boron-free AI-2 is the preferred ligand for PctA and TlpQ. AI-2 also binds to the dCACHE domains of histidine kinase KinD from Bacillus subtilis and diguanylate cyclase rpHK1S-Z16 from Rhodopseudomonas palustris, enhancing their enzymatic activities. dCACHE domains (especially those belonging to a subfamily that includes the AI-2 receptors identified in the present work) are present in a large number of bacterial and archaeal proteins. Our results support the idea that AI-2 serves as a widely used signaling molecule in the coordination of cell behavior among prokaryotic species.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes

et al. 2020

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“…• Polyamines and histamine. TSA-based ligand screening has led to the identification of two homologous receptors, TlpQ and McpU, in P. aeruginosa PAO1 and P. putida KT2440, respectively, that recognize the polyamines putrescine, cadaverine, spermidine, agmatine, ethylenediamine as well as histamine (Corral-Lugo et al, 2016;Corral-Lugo et al, 2018). The LBDs of both receptors share 62% sequence identity and, although both receptors possess the same ligand spectrum, ligands bind much tighter to TlpQ-LBD.…”

Section: Ligand-binding Studies To Individual Ligand-binding Domainsmentioning

confidence: 99%

The use of isothermal titration calorimetry to unravel chemotactic signalling mechanisms

Matilla

Martín‐Mora

Krell

2020

Environmental Microbiology

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Summary Chemotaxis is based on the action of chemosensory pathways and is typically initiated by the recognition of chemoeffectors at chemoreceptor ligand‐binding domains (LBD). Chemosensory signalling is highly complex; aspect that is not only reflected in the intricate interaction between many signalling proteins but also in the fact that bacteria frequently possess multiple chemosensory pathways and often a large number of chemoreceptors, which are mostly of unknown function. We review here the usefulness of isothermal titration calorimetry (ITC) to study this complexity. ITC is the gold standard for studying binding processes due to its precision and sensitivity, as well as its capability to determine simultaneously the association equilibrium constant, enthalpy change and stoichiometry of binding. There is now evidence that members of all major LBD families can be produced as individual recombinant proteins that maintain their ligand‐binding properties. High‐throughput screening of these proteins using thermal shift assays offer interesting initial information on chemoreceptor ligands, providing the basis for microcalorimetric analyses and microbiological experimentation. ITC has permitted the identification and characterization of many chemoreceptors with novel specificities. This ITC‐based approach can also be used to identify signal molecules that stimulate members of other families of sensor proteins.

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Histamine in cancer immunology and immunotherapy. Current status and new perspectives

Sarasola

Delgado

Nicoud

et al. 2021

Pharmacology Res & Perspec

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Cancer is the second leading cause of death globally and its incidence and mortality are rapidly increasing worldwide. The dynamic interaction of immune cells and tumor cells determines the clinical outcome of cancer. Immunotherapy comes to the forefront of cancer treatments, resulting in impressive and durable responses but only in a fraction of patients. Thus, understanding the characteristics and profiles of immune cells in the tumor microenvironment (TME) is a necessary step to move forward in the design of new immunomodulatory strategies that can boost the immune system to fight cancer. Histamine produces a complex and fine‐tuned regulation of the phenotype and functions of the different immune cells, participating in multiple regulatory responses of the innate and adaptive immunity. Considering the important actions of histamine‐producing immune cells in the TME, in this review we first address the most important immunomodulatory roles of histamine and histamine receptors in the context of cancer development and progression. In addition, this review highlights the current progress and foundational developments in the field of cancer immunotherapy in combination with histamine and pharmacological compounds targeting histamine receptors.

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High-Affinity Chemotaxis to Histamine Mediated by the TlpQ Chemoreceptor of the Human Pathogen Pseudomonas aeruginosa

Cited by 61 publications

References 82 publications

Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes

Sensing of autoinducer-2 by functionally distinct receptors in prokaryotes

The use of isothermal titration calorimetry to unravel chemotactic signalling mechanisms

Histamine in cancer immunology and immunotherapy. Current status and new perspectives

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