{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T00:40:51Z","timestamp":1791333651945,"version":"4.3.1"},"reference-count":46,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2016,3,1]],"date-time":"2016-03-01T00:00:00Z","timestamp":1456790400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc-sa\/3.0\/"},{"start":{"date-parts":[[2016,5,4]],"date-time":"2016-05-04T00:00:00Z","timestamp":1462320000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100001665","name":"Agence Nationale de la Recherche","doi-asserted-by":"publisher","award":["ANR-13-BSV8-0002-01"],"award-info":[{"award-number":["ANR-13-BSV8-0002-01"]}],"id":[{"id":"10.13039\/501100001665","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["mBio"],"published-print":{"date-parts":[[2016,5,4]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            The two-component system BvgAS controls the expression of the virulence regulon of\n            <jats:named-content content-type=\"genus-species\">Bordetella pertussis<\/jats:named-content>\n            . BvgS is a prototype of bacterial sensor kinases with extracytoplasmic Venus flytrap perception domains. Following its transmembrane segment, BvgS harbors a cytoplasmic Per-Arnt-Sim (PAS) domain and then a predicted 2-helix coiled coil that precede the dimerization-histidine-phosphotransfer domain of the kinase. BvgS homologs have a similar domain organization, or they harbor only a predicted coiled coil between the transmembrane and the dimerization-histidine-phosphotransfer domains. Here, we show that the 2-helix coiled coil of BvgS regulates the enzymatic activity in a mechanical manner. Its marginally stable hydrophobic interface enables a switch between a state of great rotational dynamics in the kinase mode and a more rigid conformation in the phosphatase mode in response to signal perception by the periplasmic domains. We further show that the activity of BvgS is controlled in the same manner if its PAS domain is replaced with the natural \u03b1-helical sequences of PAS-less homologs. Clamshell motions of the Venus flytrap domains trigger the shift of the coiled coil\u2019s dynamics. Thus, we have uncovered a general mechanism of regulation for the BvgS family of Venus flytrap-containing two-component sensor kinases.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            The two-component system BvgAS of the whooping cough agent\n            <jats:named-content content-type=\"genus-species\">Bordetella pertussis<\/jats:named-content>\n            regulates the virulence factors necessary for infection in a coordinated manner. BvgS is the prototype of a family of sensor kinase proteins found in major bacterial pathogens. When BvgS functions as a kinase,\n            <jats:named-content content-type=\"genus-species\">B. pertussis<\/jats:named-content>\n            is virulent, and the bacterium shifts to an avirulent phase after BvgS senses chemicals that make it switch to phosphatase. Our goal is to decipher the signaling mechanisms of BvgS in order to understand virulence regulation in\n            <jats:italic>Bordetella<\/jats:italic>\n            , which may lead to new antimicrobial treatments targeting those two-component systems. We discovered that the activity of BvgS is regulated in a mechanical manner. A short region of the protein that precedes the enzymatic domain switches between two states in response to signal perception by other BvgS domains. This switch region is conserved among BvgS homologs, and thus, the regulation uncovered here will likely be relevant for the family.\n          <\/jats:p>","DOI":"10.1128\/mbio.02089-15","type":"journal-article","created":{"date-parts":[[2016,3,2]],"date-time":"2016-03-02T03:03:54Z","timestamp":1456887834000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":28,"title":["Balance between Coiled-Coil Stability and Dynamics Regulates Activity of BvgS Sensor Kinase in\n            <i>Bordetella<\/i>"],"prefix":"10.1128","volume":"7","author":[{"given":"E.","family":"Lesne","sequence":"first","affiliation":[{"name":"Universit\u00e9 de Lille, INSERM, CNRS, CHU Lille, Institut Pasteur de Lille, U1019-UMR\u00a08204-CIIL, Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E.-M.","family":"Krammer","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lille, CNRS, UMR\u00a08576-UGSF, Unit\u00e9 de Glycobiologie Structurale et Fonctionnelle, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"E.","family":"Dupre","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lille, INSERM, CNRS, CHU Lille, Institut Pasteur de Lille, U1019-UMR\u00a08204-CIIL, Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"C.","family":"Locht","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lille, INSERM, CNRS, CHU Lille, Institut Pasteur de Lille, U1019-UMR\u00a08204-CIIL, Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. F.","family":"Lensink","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lille, CNRS, UMR\u00a08576-UGSF, Unit\u00e9 de Glycobiologie Structurale et Fonctionnelle, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R.","family":"Antoine","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lille, INSERM, CNRS, CHU Lille, Institut Pasteur de Lille, U1019-UMR\u00a08204-CIIL, Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5102-1704","authenticated-orcid":false,"given":"F.","family":"Jacob-Dubuisson","sequence":"additional","affiliation":[{"name":"Universit\u00e9 de Lille, INSERM, CNRS, CHU Lille, Institut Pasteur de Lille, U1019-UMR\u00a08204-CIIL, Centre d\u2019Infection et d\u2019Immunit\u00e9 de Lille, Lille, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.mib.2006.01.005"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.3184\/003685006783238308"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1369-5274(00)00070-9"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.biochem.69.1.183"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.compbiolchem.2006.09.004"},{"key":"e_1_3_2_7_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.micro.54.1.519"},{"key":"e_1_3_2_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0966-842X(03)00156-2"},{"key":"e_1_3_2_9_2","first-page":"57","volume-title":"Two-component system in bacteria","author":"Jacob-Dubuisson F","year":"2012","unstructured":"Jacob-Dubuisson F, Wintjens R, Herrou J, Dupr\u00e9 E, Antoine R. 2012. BvgS of pathogenic Bordetellae: a paradigm for sensor kinase with Venus flytrap perception domains, p 57\u201383. In Gross R, Beier D (ed), Two-component system in bacteria. 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