Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine

Acetylcholine is a central biological signal molecule present in all kingdoms of life. In humans, acetylcholine is the primary neurotransmitter of the peripheral nervous system; it mediates signal transmission at neuromuscular junctions. Here, we show that the opportunistic human pathogen Pseudomona...

Descripción completa

Detalles Bibliográficos
Autores: Matilla, Miguel A., Velando, Félix, Tajuelo, Ana, Martín-Mora, David, Xu, Wenhao, Sourjik, Victor, Gavira Gallardo, J. A., Krell, Tino
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2022
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/275869
Acceso en línea:http://hdl.handle.net/10261/275869
Access Level:acceso abierto
Palabra clave:Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
Acetylcholine
Pectobacterium atrosepticum
Quaternary amines
Neurotransmitter
id ES_f84ec02230b6dcec22e9229a0411a77f
oai_identifier_str oai:digital.csic.es:10261/275869
network_acronym_str ES
network_name_str España
repository_id_str
dc.title.none.fl_str_mv Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
title Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
spellingShingle Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
Matilla, Miguel A.
Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
Acetylcholine
Pectobacterium atrosepticum
Quaternary amines
Neurotransmitter
title_short Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
title_full Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
title_fullStr Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
title_full_unstemmed Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
title_sort Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter Acetylcholine
dc.creator.none.fl_str_mv Matilla, Miguel A.
Velando, Félix
Tajuelo, Ana
Martín-Mora, David
Xu, Wenhao
Sourjik, Victor
Gavira Gallardo, J. A.
Krell, Tino
author Matilla, Miguel A.
author_facet Matilla, Miguel A.
Velando, Félix
Tajuelo, Ana
Martín-Mora, David
Xu, Wenhao
Sourjik, Victor
Gavira Gallardo, J. A.
Krell, Tino
author_role author
author2 Velando, Félix
Tajuelo, Ana
Martín-Mora, David
Xu, Wenhao
Sourjik, Victor
Gavira Gallardo, J. A.
Krell, Tino
author2_role author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Ciencia e Innovación (España)
Junta de Andalucía
European Commission
Hessen State Ministry of Higher Education, Research and the Arts
European Synchrotron Radiation Facility
ALBA Synchrotron
Hessen State Ministry of Higher Education, Research and the Arts
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
Acetylcholine
Pectobacterium atrosepticum
Quaternary amines
Neurotransmitter
topic Chemotaxis
Chemoreceptor
Pseudomonas aeruginosa
Acetylcholine
Pectobacterium atrosepticum
Quaternary amines
Neurotransmitter
description Acetylcholine is a central biological signal molecule present in all kingdoms of life. In humans, acetylcholine is the primary neurotransmitter of the peripheral nervous system; it mediates signal transmission at neuromuscular junctions. Here, we show that the opportunistic human pathogen Pseudomonas aeruginosa exhibits chemoattraction toward acetylcholine over a concentration range of 1 mM to 100 mM. The maximal magnitude of the response was superior to that of many other P. aeruginosa chemoeffectors. We demonstrate that this chemoattraction is mediated by the PctD (PA4633) chemoreceptor. Using microcalorimetry, we show that the PctD ligand-binding domain (LBD) binds acetylcholine with a equilibrium dissociation constant (KD) of 23 mM. It also binds choline and with lower affinity betaine. Highly sensitive responses to acetylcholine and choline, and less sensitive responses to betaine and L-carnitine, were observed in Escherichia coli expressing a chimeric receptor comprising the PctD-LBD fused to the Tar chemoreceptor signaling domain. We also identified the PacA (ECA_RS10935) chemoreceptor of the phytopathogen Pectobacterium atrosepticum, which binds choline and betaine but fails to recognize acetylcholine. To identify the molecular determinants for acetylcholine recognition, we report high-resolution structures of PctD-LBD (with bound acetylcholine and choline) and PacA-LBD (with bound betaine). We identified an amino acid motif in PctD-LBD that interacts with the acetylcholine tail. This motif is absent in PacA-LBD. Significant acetylcholine chemotaxis was also detected in the plant pathogens Agrobacterium tumefaciens and Dickeya solani. To the best of our knowledge, this is the first report of acetylcholine chemotaxis and extends the range of host signals perceived by bacterial chemoreceptors.
publishDate 2022
dc.date.none.fl_str_mv 2022
2022
2022
2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/275869
url http://hdl.handle.net/10261/275869
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103972GA-I00
info:eu-repo/grantAgreement///PID2020-116261GB-I00
info:eu-repo/grantAgreement///PID2020-112612GB-I00
http://dx.doi.org/10.1128/mbio.03458-21

dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv American Society for Microbiology
publisher.none.fl_str_mv American Society for Microbiology
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869424989811245056
spelling Chemotaxis of the human pathogen Pseudomonas aeruginosa to the neurotransmitter AcetylcholineMatilla, Miguel A.Velando, FélixTajuelo, AnaMartín-Mora, DavidXu, WenhaoSourjik, VictorGavira Gallardo, J. A.Krell, TinoChemotaxisChemoreceptorPseudomonas aeruginosaAcetylcholinePectobacterium atrosepticumQuaternary aminesNeurotransmitterAcetylcholine is a central biological signal molecule present in all kingdoms of life. In humans, acetylcholine is the primary neurotransmitter of the peripheral nervous system; it mediates signal transmission at neuromuscular junctions. Here, we show that the opportunistic human pathogen Pseudomonas aeruginosa exhibits chemoattraction toward acetylcholine over a concentration range of 1 mM to 100 mM. The maximal magnitude of the response was superior to that of many other P. aeruginosa chemoeffectors. We demonstrate that this chemoattraction is mediated by the PctD (PA4633) chemoreceptor. Using microcalorimetry, we show that the PctD ligand-binding domain (LBD) binds acetylcholine with a equilibrium dissociation constant (KD) of 23 mM. It also binds choline and with lower affinity betaine. Highly sensitive responses to acetylcholine and choline, and less sensitive responses to betaine and L-carnitine, were observed in Escherichia coli expressing a chimeric receptor comprising the PctD-LBD fused to the Tar chemoreceptor signaling domain. We also identified the PacA (ECA_RS10935) chemoreceptor of the phytopathogen Pectobacterium atrosepticum, which binds choline and betaine but fails to recognize acetylcholine. To identify the molecular determinants for acetylcholine recognition, we report high-resolution structures of PctD-LBD (with bound acetylcholine and choline) and PacA-LBD (with bound betaine). We identified an amino acid motif in PctD-LBD that interacts with the acetylcholine tail. This motif is absent in PacA-LBD. Significant acetylcholine chemotaxis was also detected in the plant pathogens Agrobacterium tumefaciens and Dickeya solani. To the best of our knowledge, this is the first report of acetylcholine chemotaxis and extends the range of host signals perceived by bacterial chemoreceptors.This work was supported by grants PID2019-103972GA-I00 (to M.A.M.), PID2020-116261GB-I00 (to J.A.G.) and PID2020-112612GB-I00 (to T.K.) from the Spanish Ministry for Science and Innovation/Agencia Estatal de Investigación 10.13039/501100011033, grant P18-FR-1621 (to T.K.) from the Junta de Andalucía, by the Hessian Ministry of Higher Education, Research, and the Arts (HMWK)–LOEWE research cluster “Diffusible Signals,” subproject A1 (to V.S.), and a Peterson Group “Serving Hometown” Elites scholarship to W.X. We thank Maria Rabyk for help with the hybrid receptor cloning. We are grateful to the European Synchrotron Radiation Facility (ESRF) for the provision of time through proposals MX2281 and MX2353 and to the staff at beamlines ID30B, ID23-1, and ID30A-3 and at the Xaloc beamline of the Alba Spanish synchrotron radiation source (Barcelona) for assistance during data collection.American Society for MicrobiologyMinisterio de Ciencia e Innovación (España)Junta de AndalucíaEuropean CommissionHessen State Ministry of Higher Education, Research and the ArtsEuropean Synchrotron Radiation FacilityALBA SynchrotronHessen State Ministry of Higher Education, Research and the ArtsConsejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]2022202220222022info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionhttp://hdl.handle.net/10261/275869reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/PID2019-103972GA-I00info:eu-repo/grantAgreement///PID2020-116261GB-I00info:eu-repo/grantAgreement///PID2020-112612GB-I00http://dx.doi.org/10.1128/mbio.03458-21Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2758692026-05-22T06:33:51Z
score 15,812429