The fungal peptide toxin candidalysin induces distinct membrane repair mechanisms compared to bacterial pore-forming toxins Article Swipe
Roshan Thapa
,
Gbenga Victor Kayejo
,
Julian R. Naglik
,
Bernhard Hube
,
Peter A. Keyel
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1101/2025.05.09.653080
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1101/2025.05.09.653080
The common fungal pathogen, Candida albicans , relies on the pore-forming toxin candidalysin to damage host cells. Cells counteract pore-forming toxins by Ca 2+ -dependent mechanisms, such as microvesicle shedding and annexin recruitment to resist cholesterol-dependent cytolysins like streptolysin O (SLO), or annexin involvement and patch repair in the case of aerolysin. However, the specific Ca 2+ -dependent repair pathways engaged in response to candidalysin remain poorly understood. Here, we determined the involvement of different Ca 2+ -dependent repair mechanisms to candidalysin and compared responses to SLO and aerolysin using flow cytometry and high-resolution microscopy. We report that candidalysin triggered Ca 2+ -dependent repair, but patch repair and ceramide failed to provide significant protection. MEK-dependent repair and annexins A1, A2 and A6 contributed partially to repairing damage caused by candidalysin. However, annexin translocation after candidalysin challenge was delayed compared to SLO or aerolysin challenge. Surprisingly, extracellular Cl − improved cell survival after candidalysin challenge, but not after challenge with SLO or aerolysin. Finally, we found that candidalysin is removed via extracellular vesicle shedding. These findings reveal that Ca 2+ -dependent microvesicle shedding protects cells from candidalysin and can be engaged by multiple molecular mechanisms during membrane repair. Graphical Abstract. Candidalysin is resisted by distinct repair mechanisms compared to bacterial PFTs. After pore formation and membrane damage by each toxin, multiple repair pathways are triggered downstream of Ca²⁺ flux. Candidalysin induces a protective Cl − influx and activates MEK-dependent repair, which contributes to cell protection. Annexin translocation occurs slowly and provides minor protection, while patch repair is ineffective. In contrast, aerolysin does not benefit from Cl − influx or MEK protection. Aerolysin triggers moderate annexin translocation and relies primarily on patch repair as the main protective mechanism. Streptolysin O elicits rapid annexin translocation and activates MEK signaling, both of which contribute to robust protection. Patch repair plays only a minor protective role against SLO. The figure was created using BioRender.
Related Topics
Concepts
Pore-forming toxin
Toxin
Microbial toxins
Peptide
Microbiology
Chemistry
Membrane
Cell biology
Biophysics
Biology
Biochemistry
Metadata
- Type
- preprint
- Language
- en
- Landing Page
- https://doi.org/10.1101/2025.05.09.653080
- https://www.biorxiv.org/content/biorxiv/early/2025/05/13/2025.05.09.653080.full.pdf
- OA Status
- green
- References
- 47
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4410319383
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4410319383Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.1101/2025.05.09.653080Digital Object Identifier
- Title
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The fungal peptide toxin candidalysin induces distinct membrane repair mechanisms compared to bacterial pore-forming toxinsWork title
- Type
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preprintOpenAlex work type
- Language
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enPrimary language
- Publication year
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2025Year of publication
- Publication date
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2025-05-13Full publication date if available
- Authors
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Roshan Thapa, Gbenga Victor Kayejo, Julian R. Naglik, Bernhard Hube, Peter A. KeyelList of authors in order
- Landing page
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https://doi.org/10.1101/2025.05.09.653080Publisher landing page
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https://www.biorxiv.org/content/biorxiv/early/2025/05/13/2025.05.09.653080.full.pdfDirect link to full text PDF
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YesWhether a free full text is available
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greenOpen access status per OpenAlex
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https://www.biorxiv.org/content/biorxiv/early/2025/05/13/2025.05.09.653080.full.pdfDirect OA link when available
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Pore-forming toxin, Toxin, Microbial toxins, Peptide, Microbiology, Chemistry, Membrane, Cell biology, Biophysics, Biology, BiochemistryTop concepts (fields/topics) attached by OpenAlex
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0Total citation count in OpenAlex
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47Number of works referenced by this work
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10Other works algorithmically related by OpenAlex
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| abstract_inverted_index.The | 1, 314 |
| abstract_inverted_index.and | 31, 45, 83, 88, 93, 108, 117, 121, 187, 214, 236, 249, 276, 293 |
| abstract_inverted_index.are | 223 |
| abstract_inverted_index.but | 105, 155 |
| abstract_inverted_index.can | 188 |
| abstract_inverted_index.not | 156, 262 |
| abstract_inverted_index.the | 10, 49, 54, 72, 283 |
| abstract_inverted_index.via | 170 |
| abstract_inverted_index.was | 137, 316 |
| abstract_inverted_index.− | 148, 234, 266 |
| abstract_inverted_index.SLO. | 313 |
| abstract_inverted_index.both | 297 |
| abstract_inverted_index.case | 50 |
| abstract_inverted_index.cell | 150, 243 |
| abstract_inverted_index.does | 261 |
| abstract_inverted_index.each | 218 |
| abstract_inverted_index.flow | 91 |
| abstract_inverted_index.from | 185, 264 |
| abstract_inverted_index.host | 16 |
| abstract_inverted_index.like | 38 |
| abstract_inverted_index.main | 284 |
| abstract_inverted_index.only | 307 |
| abstract_inverted_index.pore | 212 |
| abstract_inverted_index.role | 311 |
| abstract_inverted_index.such | 27 |
| abstract_inverted_index.that | 98, 166, 177 |
| abstract_inverted_index.with | 159 |
| abstract_inverted_index.After | 211 |
| abstract_inverted_index.Cells | 18 |
| abstract_inverted_index.Here, | 69 |
| abstract_inverted_index.PFTs. | 210 |
| abstract_inverted_index.Patch | 304 |
| abstract_inverted_index.These | 174 |
| abstract_inverted_index.after | 134, 152, 157 |
| abstract_inverted_index.cells | 184 |
| abstract_inverted_index.flux. | 228 |
| abstract_inverted_index.found | 165 |
| abstract_inverted_index.minor | 251, 309 |
| abstract_inverted_index.patch | 46, 106, 254, 280 |
| abstract_inverted_index.plays | 306 |
| abstract_inverted_index.rapid | 290 |
| abstract_inverted_index.toxin | 12 |
| abstract_inverted_index.using | 90, 318 |
| abstract_inverted_index.which | 240, 299 |
| abstract_inverted_index.while | 253 |
| abstract_inverted_index.(SLO), | 41 |
| abstract_inverted_index.caused | 128 |
| abstract_inverted_index.cells. | 17 |
| abstract_inverted_index.common | 2 |
| abstract_inverted_index.damage | 15, 127, 216 |
| abstract_inverted_index.during | 195 |
| abstract_inverted_index.failed | 110 |
| abstract_inverted_index.figure | 315 |
| abstract_inverted_index.fungal | 3 |
| abstract_inverted_index.influx | 235, 267 |
| abstract_inverted_index.occurs | 247 |
| abstract_inverted_index.poorly | 67 |
| abstract_inverted_index.relies | 8, 277 |
| abstract_inverted_index.remain | 66 |
| abstract_inverted_index.repair | 47, 59, 79, 107, 116, 205, 221, 255, 281, 305 |
| abstract_inverted_index.report | 97 |
| abstract_inverted_index.resist | 35 |
| abstract_inverted_index.reveal | 176 |
| abstract_inverted_index.robust | 302 |
| abstract_inverted_index.slowly | 248 |
| abstract_inverted_index.toxin, | 219 |
| abstract_inverted_index.toxins | 21 |
| abstract_inverted_index.Annexin | 245 |
| abstract_inverted_index.Candida | 5 |
| abstract_inverted_index.Ca²⁺ | 227 |
| abstract_inverted_index.against | 312 |
| abstract_inverted_index.annexin | 32, 43, 132, 274, 291 |
| abstract_inverted_index.benefit | 263 |
| abstract_inverted_index.created | 317 |
| abstract_inverted_index.delayed | 138 |
| abstract_inverted_index.elicits | 289 |
| abstract_inverted_index.engaged | 61, 190 |
| abstract_inverted_index.induces | 230 |
| abstract_inverted_index.provide | 112 |
| abstract_inverted_index.removed | 169 |
| abstract_inverted_index.repair, | 104, 239 |
| abstract_inverted_index.repair. | 197 |
| abstract_inverted_index.vesicle | 172 |
| abstract_inverted_index.Abstract | 0 |
| abstract_inverted_index.Finally, | 163 |
| abstract_inverted_index.However, | 53, 131 |
| abstract_inverted_index.albicans | 6 |
| abstract_inverted_index.annexins | 118 |
| abstract_inverted_index.ceramide | 109 |
| abstract_inverted_index.compared | 84, 139, 207 |
| abstract_inverted_index.distinct | 204 |
| abstract_inverted_index.findings | 175 |
| abstract_inverted_index.improved | 149 |
| abstract_inverted_index.membrane | 196, 215 |
| abstract_inverted_index.moderate | 273 |
| abstract_inverted_index.multiple | 192, 220 |
| abstract_inverted_index.pathways | 60, 222 |
| abstract_inverted_index.protects | 183 |
| abstract_inverted_index.provides | 250 |
| abstract_inverted_index.resisted | 202 |
| abstract_inverted_index.response | 63 |
| abstract_inverted_index.shedding | 30, 182 |
| abstract_inverted_index.specific | 55 |
| abstract_inverted_index.survival | 151 |
| abstract_inverted_index.triggers | 272 |
| abstract_inverted_index.Abstract. | 199 |
| abstract_inverted_index.Aerolysin | 271 |
| abstract_inverted_index.Graphical | 198 |
| abstract_inverted_index.activates | 237, 294 |
| abstract_inverted_index.aerolysin | 89, 143, 260 |
| abstract_inverted_index.bacterial | 209 |
| abstract_inverted_index.challenge | 136, 158 |
| abstract_inverted_index.contrast, | 259 |
| abstract_inverted_index.cytometry | 92 |
| abstract_inverted_index.different | 75 |
| abstract_inverted_index.formation | 213 |
| abstract_inverted_index.molecular | 193 |
| abstract_inverted_index.partially | 124 |
| abstract_inverted_index.pathogen, | 4 |
| abstract_inverted_index.primarily | 278 |
| abstract_inverted_index.repairing | 126 |
| abstract_inverted_index.responses | 85 |
| abstract_inverted_index.shedding. | 173 |
| abstract_inverted_index.triggered | 100, 224 |
| abstract_inverted_index.-dependent | 25, 58, 78, 103, 180 |
| abstract_inverted_index.BioRender. | 319 |
| abstract_inverted_index.aerolysin. | 52, 162 |
| abstract_inverted_index.challenge, | 154 |
| abstract_inverted_index.challenge. | 144 |
| abstract_inverted_index.contribute | 300 |
| abstract_inverted_index.counteract | 19 |
| abstract_inverted_index.cytolysins | 37 |
| abstract_inverted_index.determined | 71 |
| abstract_inverted_index.downstream | 225 |
| abstract_inverted_index.mechanism. | 286 |
| abstract_inverted_index.mechanisms | 80, 194, 206 |
| abstract_inverted_index.protective | 232, 285, 310 |
| abstract_inverted_index.signaling, | 296 |
| abstract_inverted_index.contributed | 123 |
| abstract_inverted_index.contributes | 241 |
| abstract_inverted_index.involvement | 44, 73 |
| abstract_inverted_index.mechanisms, | 26 |
| abstract_inverted_index.microscopy. | 95 |
| abstract_inverted_index.protection, | 252 |
| abstract_inverted_index.protection. | 114, 244, 270, 303 |
| abstract_inverted_index.recruitment | 33 |
| abstract_inverted_index.significant | 113 |
| abstract_inverted_index.understood. | 68 |
| abstract_inverted_index.Candidalysin | 200, 229 |
| abstract_inverted_index.Streptolysin | 287 |
| abstract_inverted_index.candidalysin | 13, 65, 82, 99, 135, 153, 167, 186 |
| abstract_inverted_index.ineffective. | 257 |
| abstract_inverted_index.microvesicle | 29, 181 |
| abstract_inverted_index.pore-forming | 11, 20 |
| abstract_inverted_index.streptolysin | 39 |
| abstract_inverted_index.MEK-dependent | 115, 238 |
| abstract_inverted_index.Surprisingly, | 145 |
| abstract_inverted_index.candidalysin. | 130 |
| abstract_inverted_index.extracellular | 146, 171 |
| abstract_inverted_index.translocation | 133, 246, 275, 292 |
| abstract_inverted_index.high-resolution | 94 |
| abstract_inverted_index.cholesterol-dependent | 36 |
| cited_by_percentile_year | |
| countries_distinct_count | 0 |
| institutions_distinct_count | 5 |
| citation_normalized_percentile.value | 0.20075591 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |