Rita Müller, Annika König, Sabrina Groth, Robert Zarnowski, Corissa Visser, Tom Handrianz, Corinne Maufrais, Thomas Krüger, Maximilian Himmel, Sejeong Lee, Emily L Priest, Deniz Yildirim, Jonathan P Richardson, Matthew G Blango, Marie-Elisabeth Bougnoux, Olaf Kniemeyer, Christophe d'Enfert, Axel A Brakhage, David R Andes, Verena Trümper, Christian Nehls, Lydia Kasper, Selene Mogavero, Thomas Gutsmann, Julian R Naglik, Stefanie Allert, Bernhard Hube
The opportunistic fungal pathogen Candida albicans damages host cells via its peptide toxin, candidalysin. Before secretion, candidalysin is embedded in a precursor protein, Ece1, which consists of a signal peptide, the precursor of candidalysin and seven non-candidalysin Ece1 peptides (NCEPs), and is found to be conserved in clinical isolates. Here we show that the Ece1 polyprotein does not resemble the usual precursor structure of peptide toxins. C. albicans cells are not susceptible to their own toxin, and single NCEPs adjacent to candidalysin are sufficient to prevent host cell toxicity...
February 22, 2024: Nature Microbiology