The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Candidalysin is a fungal peptide toxin critical for mucosal infection
Open accessAbstract
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.
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Cites
Nonfilamentous C. albicans Mutants Are Avirulent
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Fradin, C., De Groot, P., MacCallum, D., Schaller, M., Klis, F., Odds, F. C., & Hube, B. (2005) · Molecular Microbiology · doi:10.1111/j.1365-2958.2005.04557.x · Cited by 455
Self-citationCandida albicans interactions with epithelial cells and mucosal immunity
Naglik, J. R., Moyes, D. L., Wächtler, B., & Hube, B. (2011) · Microbes and Infection · doi:10.1016/j.micinf.2011.06.009 · Cited by 277
Self-citationZhao, X., Oh, S.-H., Cheng, G., Green, C. B., Nuessen, J. A., Yeater, K., Leng, R. P., Brown, A. J. P., & Hoyer, L. L. (2004) · Microbiology · doi:10.1099/mic.0.26943-0 · Cited by 254
Wächtler, B., Citiulo, F., Jablonowski, N., Förster, S., Dalle, F., Schaller, M., Wilson, D., & Hube, B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0036952 · Cited by 250
Self-citationCandida albicans Scavenges Host Zinc via Pra1 during Endothelial Invasion
Citiulo, F., Jacobsen, I. D., Miramón, P., Schild, L., Brunke, S., Zipfel, P., Brock, M., Hube, B., & Wilson, D. (2012) · PLoS Pathogens · doi:10.1371/journal.ppat.1002777 · Cited by 242
Self-citationMunro, C. A., Bates, S., Buurman, E. T., Hughes, H. B., MacCallum, D. M., Bertram, G., Atrih, A., Ferguson, M. A. J., Bain, J. M., Brand, A., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411413200 · Cited by 200
Pardini, G., De Groot, P. W. J., Coste, A. T., Karababa, M., Klis, F. M., de Koster, C. G., & Sanglard, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606361200 · Cited by 121
Cited by
Pappas, P. G., Lionakis, M. S., Arendrup, M. C., Ostrosky-Zeichner, L., & Kullberg, B. J. (2018) · Nature Reviews Disease Primers · doi:10.1038/nrdp.2018.26 · Cited by 1,636
Candida albicans—The Virulence Factors and Clinical Manifestations of Infection
Talapko, J., Juzbašić, M., Matijević, T., Pustijanac, E., Bekić, S., Kotris, I., & Škrlec, I. (2021) · Journal of Fungi · doi:10.3390/jof7020079 · Cited by 794
“It has been shown that a hypha-specific toxin, candidalysin, is crucial for the occurrence of candidiasis [19,27].”
BackgroundHuman Anti-fungal Th17 Immunity and Pathology Rely on Cross-Reactivity against Candida albicans
Bacher, P., Hohnstein, T., Beerbaum, E., Röcker, M., Blango, M. G., Kaufmann, S., Röhmel, J., Eschenhagen, P., Grehn, C., Seidel, K., et al. (2019) · Cell · doi:10.1016/j.cell.2019.01.041 · Cited by 473
Self-citationVulvovaginal Candidiasis: A Current Understanding and Burning Questions
Willems, H. M. E., Ahmed, S. S., Liu, J., Xu, Z., & Peters, B. M. (2020) · Journal of Fungi · doi:10.3390/jof6010027 · Cited by 357
Candida parapsilosis: from genes to the bedside
Tóth, R., Nosek, J., Mora-Montes, H. M., Gabaldon, T., Bliss, J. M., Nosanchuk, J. D., Turner, S. A., Butler, G., Vágvölgyi, C., & Gácser, A. (2019) · Clinical Microbiology Reviews · doi:10.1128/cmr.00111-18 · Cited by 327
Metadata
- Authors
- Moyes, D. L., Wilson, D., Richardson, J. P., Mogavero, S., Tang, S. X., Wernecke, J., Höfs, S., Gratacap, R. L., Robbins, J., Runglall, M., Murciano, C., Blagojevic, M., Thavaraj, S., Förster, T. M., Hebecker, B., Kasper, L., Vizcay, G., Iancu, S. I., Kichik, N., Häder, A., Kurzai, O., Luo, T., Krüger, T., Kniemeyer, O., Cota, E., Bader, O., Wheeler, R. T., Gutsmann, T., Hube, B., & Naglik, J. R.
- Venue
- Nature
- Published
- 2016-03-30
- Volume
- 532
- Issue
- 7597
- Pages
- 64-68
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2329943654
- Cited by
- 942
- References
- 8
- FWCI
- 66.37
- Type
- journal article
- Language
- en
- Open access
- bronze
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