Candidalysin is a fungal peptide toxin critical for mucosal infection
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Candidalysin is a fungal peptide toxin critical for mucosal infection. / Moyes, David L; Wilson, Duncan; Richardson, Jonathan P; Mogavero, Selene; Tang, Shirley X; Wernecke, Julia; Höfs, Sarah; Gratacap, Remi L; Robbins, Jon; Runglall, Manohursingh; Murciano, Celia; Blagojevic, Mariana; Thavaraj, Selvam; Förster, Toni M; Hebecker, Betty; Kasper, Lydia; Vizcay, Gema; Iancu, Simona I; Kichik, Nessim; Häder, Antje; Kurzai, Oliver; Luo, Ting; Krüger, Thomas; Kniemeyer, Olaf; Cota, Ernesto; Bader, Oliver; Wheeler, Robert T; Gutsmann, Thomas; Hube, Bernhard; Naglik, Julian R.
in: NATURE, Jahrgang 532, Nr. 7597, 07.04.2016, S. 64-8.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Candidalysin is a fungal peptide toxin critical for mucosal infection
AU - Moyes, David L
AU - Wilson, Duncan
AU - Richardson, Jonathan P
AU - Mogavero, Selene
AU - Tang, Shirley X
AU - Wernecke, Julia
AU - Höfs, Sarah
AU - Gratacap, Remi L
AU - Robbins, Jon
AU - Runglall, Manohursingh
AU - Murciano, Celia
AU - Blagojevic, Mariana
AU - Thavaraj, Selvam
AU - Förster, Toni M
AU - Hebecker, Betty
AU - Kasper, Lydia
AU - Vizcay, Gema
AU - Iancu, Simona I
AU - Kichik, Nessim
AU - Häder, Antje
AU - Kurzai, Oliver
AU - Luo, Ting
AU - Krüger, Thomas
AU - Kniemeyer, Olaf
AU - Cota, Ernesto
AU - Bader, Oliver
AU - Wheeler, Robert T
AU - Gutsmann, Thomas
AU - Hube, Bernhard
AU - Naglik, Julian R
PY - 2016/4/7
Y1 - 2016/4/7
N2 - Cytolytic proteins and peptide toxins are classical virulence factors of several bacterial pathogens which disrupt epithelial barrier function, damage cells and activate or modulate host immune responses. Such toxins have not been identified previously in human pathogenic fungi. Here we identify the first, to our knowledge, fungal cytolytic peptide toxin in the opportunistic pathogen Candida albicans. This secreted toxin directly damages epithelial membranes, triggers a danger response signalling pathway and activates epithelial immunity. Membrane permeabilization is enhanced by a positive charge at the carboxy terminus of the peptide, which triggers an inward current concomitant with calcium influx. C. albicans strains lacking this toxin do not activate or damage epithelial cells and are avirulent in animal models of mucosal infection. We propose the name 'Candidalysin' for this cytolytic peptide toxin; a newly identified, critical molecular determinant of epithelial damage and host recognition of the clinically important fungus, C. albicans.
AB - Cytolytic proteins and peptide toxins are classical virulence factors of several bacterial pathogens which disrupt epithelial barrier function, damage cells and activate or modulate host immune responses. Such toxins have not been identified previously in human pathogenic fungi. Here we identify the first, to our knowledge, fungal cytolytic peptide toxin in the opportunistic pathogen Candida albicans. This secreted toxin directly damages epithelial membranes, triggers a danger response signalling pathway and activates epithelial immunity. Membrane permeabilization is enhanced by a positive charge at the carboxy terminus of the peptide, which triggers an inward current concomitant with calcium influx. C. albicans strains lacking this toxin do not activate or damage epithelial cells and are avirulent in animal models of mucosal infection. We propose the name 'Candidalysin' for this cytolytic peptide toxin; a newly identified, critical molecular determinant of epithelial damage and host recognition of the clinically important fungus, C. albicans.
KW - Calcium
KW - Candida albicans
KW - Candidiasis
KW - Cell Membrane Permeability
KW - Cytotoxins
KW - Epithelial Cells
KW - Fungal Proteins
KW - Host-Pathogen Interactions
KW - Humans
KW - Mucous Membrane
KW - Mycotoxins
KW - Signal Transduction
KW - Virulence
KW - Virulence Factors
KW - Journal Article
KW - Research Support, N.I.H., Extramural
KW - Research Support, Non-U.S. Gov't
U2 - 10.1038/nature17625
DO - 10.1038/nature17625
M3 - SCORING: Journal article
C2 - 27027296
VL - 532
SP - 64
EP - 68
JO - NATURE
JF - NATURE
SN - 0028-0836
IS - 7597
ER -