{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T09:34:24Z","timestamp":1791192864883,"version":"4.1.0"},"reference-count":66,"publisher":"American Society for Microbiology","issue":"9","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["J. Bacteriol."],"published-print":{"date-parts":[[2015,5,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title><jats:p>Listeriae take up glucose and mannose predominantly through a mannose class phosphoenolpyruvate:carbohydrate phosphotransferase system (PTS<jats:sup>Man<\/jats:sup>), whose three components are encoded by the<jats:italic>manLMN<\/jats:italic>genes. The expression of these genes is controlled by ManR, a LevR-type transcription activator containing two PTS regulation domains (PRDs) and two PTS-like domains (enzyme IIA<jats:sup>Man<\/jats:sup>[EIIA<jats:sup>Man<\/jats:sup>]- and EIIB<jats:sup>Gat<\/jats:sup>-like). We demonstrate here that in<jats:named-content content-type=\"genus-species\">Listeria monocytogenes<\/jats:named-content>, ManR is activated via the phosphorylation of His585 in the EIIA<jats:sup>Man<\/jats:sup>-like domain by the general PTS components enzyme I and HPr. We also show that ManR is regulated by the PTS<jats:sup>Mpo<\/jats:sup>and that EIIB<jats:sup>Mpo<\/jats:sup>plays a dual role in ManR regulation. First, yeast two-hybrid experiments revealed that unphosphorylated EIIB<jats:sup>Mpo<\/jats:sup>interacts with the two C-terminal domains of ManR (EIIB<jats:sup>Gat<\/jats:sup>-like and PRD2) and that this interaction is required for ManR activity. Second, in the absence of glucose\/mannose, phosphorylated EIIB<jats:sup>Mpo<\/jats:sup>(P\u223cEIIB<jats:sup>Mpo<\/jats:sup>) inhibits ManR activity by phosphorylating His871 in PRD2. The presence of glucose\/mannose causes the dephosphorylation of P\u223cEIIB<jats:sup>Mpo<\/jats:sup>and P\u223cPRD2 of ManR, which together lead to the induction of the<jats:italic>manLMN<\/jats:italic>operon. Complementation of a \u0394<jats:italic>manR<\/jats:italic>mutant with various<jats:italic>manR<\/jats:italic>alleles confirmed the antagonistic effects of PTS-catalyzed phosphorylation at the two different histidine residues of ManR. Deletion of<jats:italic>manR<\/jats:italic>prevented not only the expression of the<jats:italic>manLMN<\/jats:italic>operon but also glucose-mediated repression of virulence gene expression; however, repression by other carbohydrates was unaffected. Interestingly, the expression of<jats:italic>manLMN<\/jats:italic>in<jats:named-content content-type=\"genus-species\">Listeria innocua<\/jats:named-content>was reported to require not only ManR but also the Crp-like transcription activator Lin0142. Unlike Lin0142, the<jats:named-content content-type=\"genus-species\">L. monocytogenes<\/jats:named-content>homologue, Lmo0095, is not required for<jats:italic>manLMN<\/jats:italic>expression; its absence rather stimulates<jats:italic>man<\/jats:italic>expression.<\/jats:p><jats:p><jats:bold>IMPORTANCE<\/jats:bold><jats:named-content content-type=\"genus-species\">Listeria monocytogenes<\/jats:named-content>is a human pathogen causing the foodborne disease listeriosis. The expression of most virulence genes is controlled by the transcription activator PrfA. Its activity is strongly repressed by carbohydrates, including glucose, which is transported into<jats:named-content content-type=\"genus-species\">L. monocytogenes<\/jats:named-content>mainly via a mannose\/glucose-specific phosphotransferase system (PTS<jats:sup>Man<\/jats:sup>). Expression of the<jats:italic>man<\/jats:italic>operon is regulated by the transcription activator ManR, the activity of which is controlled by a second, low-efficiency PTS of the mannose family, which functions as glucose sensor. Here we demonstrate that the EIIB<jats:sup>Mpo<\/jats:sup>component plays a dual role in ManR regulation: it inactivates ManR by phosphorylating its His871 residue and stimulates ManR by interacting with its two C-terminal domains.<\/jats:p>","DOI":"10.1128\/jb.02522-14","type":"journal-article","created":{"date-parts":[[2015,2,18]],"date-time":"2015-02-18T08:16:48Z","timestamp":1424247408000},"page":"1559-1572","source":"Crossref","is-referenced-by-count":18,"title":["Interaction with Enzyme IIB<sup>Mpo<\/sup>(EIIB<sup>Mpo<\/sup>) and Phosphorylation by Phosphorylated EIIB<sup>Mpo<\/sup>Exert Antagonistic Effects on the Transcriptional Activator ManR of Listeria monocytogenes"],"prefix":"10.1128","volume":"197","author":[{"given":"Arthur Constant","family":"Z\u00e9br\u00e9","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francine Moussan","family":"Ak\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magali","family":"Ventroux","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rose","family":"Koffi-Nevry","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marie-Fran\u00e7oise","family":"Noirot-Gros","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Josef","family":"Deutscher","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eliane","family":"Milohanic","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","published-online":{"date-parts":[[2015,2,17]]},"reference":[{"key":"key20180919081453_B1","doi-asserted-by":"crossref","first-page":"498","DOI":"10.1128\/JB.180.3.498-504.1998","article-title":"Characterization of glucose-specific catabolite repression-resistant mutants of Bacillus subtilis: identification of a novel hexose:H+ symporter","volume":"180","year":"1998","journal-title":"J Bacteriol"},{"key":"key20180919081453_B2","doi-asserted-by":"crossref","first-page":"4929","DOI":"10.1128\/JB.181.16.4929-4936.1999","article-title":"Identification of a gene in Staphylococcus xylosus encoding a novel glucose uptake protein","volume":"181","year":"1999","journal-title":"J Bacteriol"},{"key":"key20180919081453_B3","doi-asserted-by":"publisher","first-page":"939","DOI":"10.1128\/MMBR.00024-06","article-title":"How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria","volume":"70","year":"2006","journal-title":"Microbiol Mol Biol Rev"},{"key":"key20180919081453_B4","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1021\/bi00325a023","article-title":"Phosphoenolpyruvate-dependent protein kinase enzyme I of Streptococcus faecalis. 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