{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,21]],"date-time":"2026-03-21T02:50:21Z","timestamp":1774061421251,"version":"3.50.1"},"reference-count":112,"publisher":"Frontiers Media SA","license":[{"start":{"date-parts":[[2021,9,22]],"date-time":"2021-09-22T00:00:00Z","timestamp":1632268800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["frontiersin.org"],"crossmark-restriction":true},"short-container-title":["Front. Cell. Infect. Microbiol."],"abstract":"<jats:p><jats:italic>Pseudomonas aeruginosa<\/jats:italic> is a major opportunistic human pathogen which employs a myriad of virulence factors. In people with cystic fibrosis (CF) <jats:italic>P. aeruginosa<\/jats:italic> frequently colonises the lungs and becomes a chronic infection that evolves to become less virulent over time, but often adapts to favour persistence in the host with alginate-producing mucoid, slow-growing, and antibiotic resistant phenotypes emerging. Cysteamine is an endogenous aminothiol which has been shown to prevent biofilm formation, reduce phenazine production, and potentiate antibiotic activity against <jats:italic>P. aeruginosa<\/jats:italic>, and has been investigated in clinical trials as an adjunct therapy for pulmonary exacerbations of CF.\u00a0Here we demonstrate (for the first time in a prokaryote) that cysteamine prevents glycine utilisation by <jats:italic>P. aeruginosa<\/jats:italic> in common with previously reported activity blocking the glycine cleavage system in human cells. Despite the clear inhibition of glycine metabolism, cysteamine also inhibits hydrogen cyanide (HCN) production by <jats:italic>P. aeruginosa<\/jats:italic>, suggesting a direct interference in the regulation of virulence factor synthesis. Cysteamine impaired chemotaxis, lowered pyocyanin, pyoverdine and exopolysaccharide production, and reduced the toxicity of <jats:italic>P. aeruginosa<\/jats:italic> secreted factors in a <jats:italic>Galleria mellonella<\/jats:italic> infection model. Thus, cysteamine has additional potent anti-virulence properties targeting <jats:italic>P. aeruginosa<\/jats:italic>, further supporting its therapeutic potential in CF and other infections.<\/jats:p>","DOI":"10.3389\/fcimb.2021.718213","type":"journal-article","created":{"date-parts":[[2021,9,22]],"date-time":"2021-09-22T06:23:24Z","timestamp":1632291804000},"update-policy":"https:\/\/doi.org\/10.3389\/crossmark-policy","source":"Crossref","is-referenced-by-count":16,"title":["Cysteamine Inhibits Glycine Utilisation and Disrupts Virulence in Pseudomonas aeruginosa"],"prefix":"10.3389","volume":"11","author":[{"given":"Douglas J.","family":"Fraser-Pitt","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Stephen K.","family":"Dolan","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David","family":"Toledo-Aparicio","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jessica G.","family":"Hunt","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Daniel W.","family":"Smith","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Niamh","family":"Lacy-Roberts","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Piumi Sara","family":"Nupe Hewage","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Teodora N.","family":"Stoyanova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Erin","family":"Manson","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevin","family":"McClean","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Neil F.","family":"Inglis","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Derry K.","family":"Mercer","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Deborah A.","family":"O\u2019Neil","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1965","published-online":{"date-parts":[[2021,9,22]]},"reference":[{"key":"B1","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1107\/S1744309105001545","article-title":"Mdab From Escherichia Coli: Cloning, Purification, Crystallization and Preliminary X-Ray Analysis","volume":"61","author":"Adams","year":"2005","journal-title":"Acta Crystallogr. 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