The Endoplasmic Reticulum-Mitochondrion Tether ERMES Orchestrates Fungal Immune Evasion, Illuminating Inflammasome Responses to Hyphal Signals
Open accessAbstract
The pathogenic yeast Candida albicans escapes macrophages by triggering NLRP3 inflammasome-dependent host cell death (pyroptosis). Pyroptosis is inflammatory and must be tightly regulated by host and microbe, but the mechanism is incompletely defined. We characterized the C. albicans endoplasmic reticulum (ER)-mitochondrion tether ERMES and show that the ERMES mmm1 mutant is severely crippled in killing macrophages despite hyphal formation and normal phagocytosis and survival. To understand dynamic inflammasome responses to Candida with high spatiotemporal resolution, we established live-cell imaging for parallel detection of inflammasome activation and pyroptosis at the single-cell level. This showed that the inflammasome response to mmm1 mutant hyphae is delayed by 10 h, after which an exacerbated activation occurs. The NLRP3 inhibitor MCC950 inhibited inflammasome activation and pyroptosis by C. albicans, including exacerbated inflammasome activation by the mmm1 mutant. At the cell biology level, inactivation of ERMES led to a rapid collapse of mitochondrial tubular morphology, slow growth and hyphal elongation at host temperature, and reduced exposed 1,3-β-glucan in hyphal populations. Our data suggest that inflammasome activation by C. albicans requires a signal threshold dependent on hyphal elongation and cell wall remodeling, which could fine-tune the response relative to the level of danger posed by C. albicans. The phenotypes of the ERMES mutant and the lack of conservation in animals suggest that ERMES is a promising antifungal drug target. Our data further indicate that NLRP3 inhibition by MCC950 could modulate C. albicans-induced inflammation. IMPORTANCE The yeast Candida albicans causes human infections that have mortality rates approaching 50%. The key to developing improved therapeutics is to understand the host-pathogen interface. A critical interaction is that with macrophages: intracellular Candida triggers the NLRP3/caspase-1 inflammasome for escape through lytic host cell death, but this also activates antifungal responses. To better understand how the inflammasome response to Candida is fine-tuned, we established live-cell imaging of inflammasome activation at single-cell resolution, coupled with analysis of the fungal ERMES complex, a mitochondrial regulator that lacks human homologs. We show that ERMES mediates Candida escape via inflammasome-dependent processes, and our data suggest that inflammasome activation is controlled by the level of hyphal growth and exposure of cell wall components as a proxy for severity of danger. Our study provides the most detailed dynamic analysis of inflammasome responses to a fungal pathogen so far and establishes promising pathogen- and host-derived therapeutic strategies.
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The ERMES complex was found to be involved in Candida albicans and Aspergillus fumigatus pathogenicity, suggesting its potential as a target for new antifungal drugs.
“The ERMES complex was found to be involved in C. albicans and A. fumigatus pathogenicity, suggesting its potential as a target for new antifungal drugs [34,35,36].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [35]
The Introduction and Results link ERMES to C. albicans virulence and macrophage immune evasion. The Discussion’s “Conclusions and outlook” identifies ERMES as promising for antifungal drug discovery, but for A. fumigatus it mentions mitochondrial morphology in virulence-related processes—not a demonstrated role for ERMES itself. Our copy provides no page numbers for these passages. (LLM, conf=0.87)
Experimental — accuracy not yet measuredIn Candida albicans, the ERMES complex is involved in immune system evasion and cell wall stress responses.
“In C. albicans, the ERMES complex is involved in immune system evasion [35] and cell wall stress responses [34].”
From In Candida glabrata, ERMES Component GEM1 Controls Mitochondrial Morphology, mtROS, and Drug Efflux Pump Expression, Resulting in Azole Susceptibility (2023) · cites this paper as [35]
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Cites
Hidden Killers: Human Fungal Infections
Brown, G. D., Denning, D. W., Gow, N. A. R., Levitz, S. M., Netea, M. G., & White, T. C. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3004404 · Cited by 4,284 · cited 1× · see citing works
“The yeast Candida albicans is the most common fungal pathogen in human infections, and it can cause deadly systemic disease (4).”
Amplification efficiency: linking baseline and bias in the analysis of quantitative PCR data
Ruijter, J. M., Ramakers, C., Hoogaars, W. M. H., Karlen, Y., Bakker, O., van den Hoff, M. J. B., & Moorman, A. F. M. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp045 · Cited by 3,043 · cited 1× · see citing works
“Data analysis was done using LinReg software (57).”
A small-molecule inhibitor of the NLRP3 inflammasome for the treatment of inflammatory diseases
Coll, R. C., Robertson, A. A. B., Chae, J. J., Higgins, S. C., Muñoz-Planillo, R., Inserra, M. C., Vetter, I., Dungan, L. S., Monks, B. G., Stutz, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3806 · Cited by 2,849 · see citing works
Self-citationNonfilamentous C. albicans Mutants Are Avirulent
Lo, H.-J., Köhler, J. R., DiDomenico, B., Loebenberg, D., Cacciapuoti, A., & Fink, G. R. (1997) · Cell · doi:10.1016/s0092-8674(00)80358-x · Cited by 1,809 · cited 1× · see citing works
“Furthermore, metabolism is involved in the transition of C. albicans from yeast to hyphal morphology, which promotes immune evasion by causing host cell lysis (9–12).”
Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria
Miao, E. A., Leaf, I. A., Treuting, P. M., Mao, D. P., Dors, M., Sarkar, A., Warren, S. E., Wewers, M. D., & Aderem, A. (2010) · Nature Immunology · doi:10.1038/ni.1960 · Cited by 1,336 · cited 1× · see citing works
“Pyroptosis exposes intracellular pathogens to immune attack and rids them of their replication niche (15).”
An ER-Mitochondria Tethering Complex Revealed by a Synthetic Biology Screen
Kornmann, B., Currie, E., Collins, S. R., Schuldiner, M., Nunnari, J., Weissman, J. S., & Walter, P. (2009) · Science · doi:10.1126/science.1175088 · Cited by 1,275 · cited 2× · see citing works
“Studies in S. cerevisiae suggested roles for ERMES not only in mitochondrial morphology but also in mitochondrial lipid homeostasis, fitness, and respiration through maintenance of the mitochondrial genome (20, 27–34).”
Candidalysin is a fungal peptide toxin critical for mucosal infection
Moyes, D. L., Wilson, D., Richardson, J. P., Mogavero, S., Tang, S. X., Wernecke, J., Hoefs, S., Gratacap, R. L., Robbins, J., Runglall, M., et al. (2016) · Nature · doi:10.1038/nature17625 · Cited by 928 · cited 1× · see citing works
“…of exposed 1,3-(cid:2) -glucan and moderately reduced expression of HWP1 and PHR1 encoding a hypha-specific cell wall adhesin and a cell wall-remodeling enzyme, respectively, as well as ECE1 , a hypha-specific gene that was recently shown to encode a toxin that can cause damage to epithelia (46).”
Candida albicans morphogenesis and host defence: discriminating invasion from colonization
Gow, N. A. R., van de Veerdonk, F. L., Brown, A. J. P., & Netea, M. G. (2012) · Nature Reviews Microbiology · doi:10.1038/nrmicro2711 · Cited by 888 · cited 1× · see citing works
“…that C. albicans induces pyroptosis after the expression of virulence traits that may be important for extracellular survival and dissemination under inflammatory conditions, as activation of the NLRP3 inflam-masome also triggers antifungal immune responses (reviewed in references 17 and 18).”
The adaptor ASC has extracellular and 'prionoid' activities that propagate inflammation
Franklin, B. S., Bossaller, L., De Nardo, D., Ratter, J. M., Stutz, A., Engels, G., Brenker, C., Nordhoff, M., Mirandola, S. R., Al-Amoudi, A., et al. (2014) · Nature Immunology · doi:10.1038/ni.2913 · Cited by 773 · cited 3× · see citing works
“The immortalized mCerulean-tagged ASC inflammasome reporter macrophages were a gift from Eicke Latz (36).”
Transcriptional Response of <i>Candida albicans</i> upon Internalization by Macrophages
Lorenz, M. C., Bender, J. A., & Fink, G. R. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.5.1076-1087.2004 · Cited by 712 · cited 1× · see citing works
“albicans reprograms its metabolism to suit the nutrient environment in phagocytes (7, 8).”
Immune defence against Candida fungal infections
Netea, M. G., Joosten, L. A. B., van der Meer, J. W. M., Kullberg, B.-J., & van de Veerdonk, F. L. (2015) · Nature Reviews Immunology · doi:10.1038/nri3897 · Cited by 642 · cited 1× · see citing works
“…that C. albicans induces pyroptosis after the expression of virulence traits that may be important for extracellular survival and dissemination under inflammatory conditions, as activation of the NLRP3 inflam-masome also triggers antifungal immune responses (reviewed in references 17 and 18).”
Are pathogenic bacteria just looking for food? Metabolism and microbial pathogenesis
Rohmer, L., Hocquet, D., & Miller, S. I. (2011) · Trends in Microbiology · doi:10.1016/j.tim.2011.04.003 · Cited by 364 · cited 1× · see citing works
“KEYWORDS: Candida albicans , macrophage, metabolism, mitochondria I mportant aspects of microbial pathogenesis involve metabolic adaptation in the host (1–3).”
MAPK, MKP1 and c-Fos Discriminate Candida albicans Yeast from Hyphae in Epithelial Cells
Moyes, D., Runglall, M., Murciano, C., Shen, C., Nayar, D., Thavaraj, S., Kohli, A., Islam, A., Mora-Montes, H., Challacombe, S., et al. (2010) · Cell Host and Microbe · doi:10.1016/j.chom.2010.08.002 · Cited by 347 · see citing works
Higher-Order Assemblies in a New Paradigm of Signal Transduction
Wu, H. (2013) · Cell · doi:10.1016/j.cell.2013.03.013 · Cited by 346 · cited 1× · see citing works
“As discussed in a recent review, threshold mechanisms of signaling allow for sensitive responses tailored to the level of threat, thereby minimizing noisy inflammatory responses that could be detrimental to the host (49).”
ASC Speck Formation as a Readout for Inflammasome Activation
Stutz, A., Horvath, G. L., Monks, B. G., & Latz, E. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-523-1_8 · Cited by 335 · cited 3× · see citing works
“Given that ASC-Cerulean is an immortalized cell line in which NLRP3 and ASC are overexpressed (37), it was important to optimize the infection conditions to closely mimic the response observed in primary BMDMs. Optimization identified that at a multiplicity of 3 Candida cells to 1 macrophage,…”
Murley, A., Lackner, L. L., Osman, C., West, M., Voeltz, G. K., Walter, P., & Nunnari, J. (2013) · eLife · doi:10.7554/elife.00422 · Cited by 326 · see citing works
Genetic and phenotypic intra-species variation in <i>Candida albicans</i>
Hirakawa, M. P., Martinez, D. A., Sakthikumar, S., Anderson, M. Z., Berlin, A., Gujja, S., Zeng, Q., Zisson, E., Wang, J. M., Greenberg, J. M., et al. (2015) · Genome Research · doi:10.1101/gr.174623.114 · Cited by 320 · cited 1× · see citing works
“extreme end, being a highly filamentous strain (50).”
Cutting Edge: <i>Candida albicans</i> Hyphae Formation Triggers Activation of the Nlrp3 Inflammasome
Joly, S., Ma, N., Sadler, J. J., Soll, D. R., Cassel, S. L., & Sutterwala, F. S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901323 · Cited by 296 · cited 2× · see citing works
“In the case of C. albicans , this means that not only does the inflammasome discriminate yeast from hyphal morphology (16) but the response is more sensitively fine-tuned to hyphal growth levels, which could allow for tight regulation.”
Osman, C., Haag, M., Potting, C., Rodenfels, J., Dip, P. V., Wieland, F., Brügger, B., Westermann, B., & Langer, T. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200810189 · Cited by 295 · cited 1× · see citing works
“Studies in S. cerevisiae suggested roles for ERMES not only in mitochondrial morphology but also in mitochondrial lipid homeostasis, fitness, and respiration through maintenance of the mitochondrial genome (20, 27–34).”
Sogo, L. F., & Yaffe, M. P. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1361 · Cited by 284 · cited 2× · see citing works
“Studies in S. cerevisiae suggested roles for ERMES not only in mitochondrial morphology but also in mitochondrial lipid homeostasis, fitness, and respiration through maintenance of the mitochondrial genome (20, 27–34).”
Boldogh, I., Nowakowski, D. W., Yang, H.-C., Chung, H., Karmon, S., Royes, P., & Pon, L. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e03-04-0225 · Cited by 283 · see citing works
(1,3)-β-Glucans Activate Both Dectin-1 and NLRP3 Inflammasome in Human Macrophages
Kankkunen, P., Teirilä, L., Rintahaka, J., Alenius, H. T., Wolff, H. J., & Matikainen, S. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903019 · Cited by 274 · see citing works
The Pathogen Candida albicans Hijacks Pyroptosis for Escape from Macrophages
Uwamahoro, N., Verma-Gaur, J., Shen, H.-H., Qu, Y., Lewis, R., Lu, J., Bambery, K., Masters, S. L., Vince, J. E., Naderer, T., et al. (2014) · mBio · doi:10.1128/mbio.00003-14 · Cited by 264 · cited 11× · see citing works
“This is consistent with substantial escape of the control Candida strain from macrophages, as most fungal growth under these conditions is seen after hyphae lyse macrophages and egress into the surrounding medium (see Movie S1).”
InfluentialMetabolism impacts upon Candida immunogenicity and pathogenicity at multiple levels
Brown, A. J. P., Brown, G. D., Netea, M. G., & Gow, N. A. R. (2014) · Trends in Microbiology · doi:10.1016/j.tim.2014.07.001 · Cited by 258 · cited 2× · see citing works
“For C. albicans , metabolic regulation has wide-ranging consequences for virulence, including interaction with host immunity and resistance to stressors and antifungal therapeutics (reviewed in reference 3).”
Burgess, S. M., Delannoy, M., & Jensen, R. E. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.6.1375 · Cited by 249 · see citing works
Global analysis of fungal morphology exposes mechanisms of host cell escape
O’Meara, T. R., Veri, A. O., Ketela, T., Jiang, B., Roemer, T., & Cowen, L. E. (2015) · Nature Communications · doi:10.1038/ncomms7741 · Cited by 243 · cited 2× · see citing works
“albicans is tightly regulated remains to be fully understood, particularly in light of recent studies that showed that factors other than fungal morphology are at play, and yeast cells can also cause inflammasomedependent macrophage lysis under some conditions (13, 14, 19).”
The Emerging Network of Mitochondria-Organelle Contacts
Murley, A., & Nunnari, J. M. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.01.031 · Cited by 236 · cited 1× · see citing works
“Complexes such as ERMES, which mediate interactions between organelles by providing “membrane contact sites,” represent hubs that can control cell physiology on a global level (21, 22).”
Candida albicans Triggers NLRP3-Mediated Pyroptosis in Macrophages
Wellington, M., Koselny, K., Sutterwala, F. S., & Krysan, D. J. (2014) · Eukaryotic Cell · doi:10.1128/ec.00336-13 · Cited by 227 · cited 7× · see citing works
“On the pathogen side, filamentous growth has been linked to inflammasome activation and pyroptosis (13, 14, 16).”
InfluentialHobbs, A. E. A., Srinivasan, M., McCaffery, J., & Jensen, R. (2001) · Journal of Cell Biology · doi:10.1083/jcb.152.2.401 · Cited by 223 · see citing works
Shingu-Vazquez, M., & Traven, A. (2011) · Eukaryotic Cell · doi:10.1128/ec.05184-11 · Cited by 209 · see citing works
Self-citationNaglik, J. R., Rodgers, C. A., Shirlaw, P. J., Dobbie, J. L., Fernandes‐Naglik, L. L., Greenspan, D., Agabian, N., & Challacombe, S. J. (2003) · The Journal of Infectious Diseases · doi:10.1086/376536 · Cited by 206 · cited 1× · see citing works
“All primers used for quantitative RT-PCR are listed in Table S3 in the supplemental material, and some are further described in references 55 and 56.”
ERMES-mediated ER-mitochondria contacts: molecular hubs for the regulation of mitochondrial biology
Kornmann, B., & Walter, P. (2010) · Journal of Cell Science · doi:10.1242/jcs.058636 · Cited by 205 · cited 1× · see citing works
“Complexes such as ERMES, which mediate interactions between organelles by providing “membrane contact sites,” represent hubs that can control cell physiology on a global level (21, 22).”
BackgroundConserved SMP domains of the ERMES complex bind phospholipids and mediate tether assembly
AhYoung, A. P., Jiang, J., Zhang, J., Dang, X. K., Loo, J. A., Zhou, Z. H., & Egea, P. F. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422363112 · Cited by 197 · cited 1× · see citing works
“Recent work has shown that Mmm1 and Mdm12 associate as a heterotetramer and that Mdm34 also forms dimers (58), but for simplicity, we do not depict it here.”
Berger, K. H., Sogo, L. F., & Yaffe, M. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.136.3.545 · Cited by 197 · see citing works
Cheng, S.-C., van de Veerdonk, F. L., Lenardon, M., Stoffels, M., Plantinga, T., Smeekens, S., Rizzetto, L., Mukaremera, L., Preechasuth, K., Cavalieri, D., et al. (2011) · Journal of Leukocyte Biology · doi:10.1189/jlb.1210702 · Cited by 191 · cited 2× · see citing works
“Mitochondrial activity is needed for cell wall integrity in C. albicans (39–41; reviewed in references 5 and 6), and cell wall components, including 1,3-(cid:2) -glucan and cell wall mannosylation, correlate with inflammasome activation and pyroptosis (13, 19, 42–44).”
Vylkova, S., & Lorenz, M. C. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1003995 · Cited by 174 · see citing works
Kumar, H., Kumagai, Y., Tsuchida, T., Koenig, P.-A., Satoh, T. K., Guo, Z., Jang, M. H., Saitoh, T., Akira, S., & Kawai, T. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0902477 · Cited by 172 · see citing works
Ghosh, S., Navarathna, D. H. M. L. P., Roberts, D. D., Cooper, J. T., Atkin, A. L., Petro, T. M., & Nickerson, K. W. (2009) · Infection and Immunity · doi:10.1128/iai.01452-08 · Cited by 165 · see citing works
Single-Cell Imaging of Caspase-1 Dynamics Reveals an All-or-None Inflammasome Signaling Response
Liu, T., Yamaguchi, Y., Shirasaki, Y., Shikada, K., Yamagishi, M., Hoshino, K., Kaisho, T., Takemoto, K., Suzuki, T., Kuranaga, E., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.012 · Cited by 150 · cited 3× · see citing works
“Consistent with our proposition for a signal threshold model are recent data of caspase-1 activation in response to Salmonella , or signals such as the NLRP3 activator silica, which showed “digital” or threshold signaling (38).”
InfluentialYoungman, M. J., Hobbs, A. E. A., Burgess, S. M., Srinivasan, M., & Jensen, R. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200308012 · Cited by 148 · see citing works
Pathway analysis of Candida albicans survival and virulence determinants in a murine infection model
Becker, J. M., Kauffman, S., Hauser, M., Huang, L.-Y., Lin, M. T.-Y., Sillaots, S., Jiang, B., Xu, D., & Roemer, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009845107 · Cited by 135 · cited 3× · see citing works
“further explains the role of MMM1 in systemic virulence in mutant library screens (24).”
InfluentialLowman, D. W., Greene, R. R., Bearden, D. W., Kruppa, M., Pottier, M., Monteiro, M. A., Soldatov, D. V., Ensley, H. E., Cheng, S., Netea, M. G., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.529131 · Cited by 133 · cited 1× · see citing works
“of interleukin-1 (IL-1 ) secretion as a proxy for caspase-1 activation (48).”
Dagley, M. J., Gentle, I. E., Beilharz, T. H., Pettolino, F. A., Djordjevic, J. T., Lo, T. L., Uwamahoro, N., Rupasinghe, T., Tull, D. L., McConville, M., et al. (2011) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07503.x · Cited by 128 · see citing works
Self-citationThomas, E., Roman, E., Claypool, S., Manzoor, N., Pla, J., & Panwar, S. L. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00889-13 · Cited by 105 · cited 1× · see citing works
“In addition to C. albicans (this study and reference 51), mitochondrial morphology has been implicated in virulence-related processes in Cryptococcus gattii (52) and Aspergillus fumigatus (53).”
The Ancient and Widespread Nature of the ER–Mitochondria Encounter Structure
Wideman, J. G., Gawryluk, R. M. R., Gray, M. W., & Dacks, J. B. (2013) · Molecular Biology and Evolution · doi:10.1093/molbev/mst120 · Cited by 102 · cited 2× · see citing works
“Due to its absence in humans (23) and a key role in maintaining the”
System-level impact of mitochondria on fungal virulence: to metabolism and beyond
Calderone, R., Li, D., & Traven, A. (2015) · FEMS Yeast Research · doi:10.1093/femsyr/fov027 · Cited by 101 · cited 2× · see citing works
“In eukaryotic cells, mitochondria have central functions in energy production and metabolism, and mitochondrial function is necessary for virulence of pathogenic fungi (reviewed in references 5 and 6).”
‘Division of labour’ in response to host oxidative burst drives a fatal Cryptococcus gattii outbreak
Voelz, K., Johnston, S. A., Taylor-Smith, L. M., Hall, R. A., Idnurm, A., & May, R. C. (2014) · Nature Communications · doi:10.1038/ncomms6194 · Cited by 101 · cited 1× · see citing works
“implicated in virulence-related processes in Cryptococcus gattii (52) and Aspergillus”
Fungal Immune Evasion in a Model Host–Pathogen Interaction: Candida albicans Versus Macrophages
Jiménez-López, C., & Lorenz, M. C. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003741 · Cited by 91 · cited 1× · see citing works
“albicans reprograms its metabolism to suit the nutrient environment in phagocytes (7, 8).”
Baruch, M., Belotserkovsky, I., Hertzog, B. B., Ravins, M., Dov, E., McIver, K. S., Breton, Y. S. L., Zhou, Y., Cheng, C. Y., & Hanski, E. (2014) · Cell · doi:10.1016/j.cell.2013.12.007 · Cited by 85 · see citing works
Neubauer, M., Zhu, Z., Penka, M., Helmschrott, C., Wagener, N., & Wagener, J. (2015) · Molecular Microbiology · doi:10.1111/mmi.13167 · Cited by 76 · cited 1× · see citing works
“In addition to C. albicans (this study and reference 51), mitochondrial morphology has been implicated in virulence-related processes in Cryptococcus gattii (52) and Aspergillus fumigatus (53).”
Jiménez-López, C., Collette, J. R., Brothers, K. M., Shepardson, K. M., Cramer, R. A., Wheeler, R. T., & Lorenz, M. C. (2012) · Eukaryotic Cell · doi:10.1128/ec.00290-12 · Cited by 72 · see citing works
Candida albicans Morphogenesis Is Not Required for Macrophage Interleukin 1β Production
Wellington, M. A., Koselny, K., & Krysan, D. J. (2012) · mBio · doi:10.1128/mbio.00433-12 · Cited by 67 · cited 1× · see citing works
“Previous studies have reported on mutants that had much milder phenotypes (13), or macrophage death was assessed only at one, early time point (4 or 5 h postinfection) (14, 19, 35).”
Qu, Y., Jelicic, B., Pettolino, F., Perry, A., Lo, T. L., Hewitt, V. L., Bantun, F., Beilharz, T. H., Peleg, A. Y., Lithgow, T., et al. (2012) · Eukaryotic Cell · doi:10.1128/ec.05292-11 · Cited by 57 · cited 1× · see citing works
“In C. albicans , mitochondrial dysfunction can have large effects on fitness (for example, see reference 26).”
Self-citationShe, X., Khamooshi, K., Gao, Y., Shen, Y., Lv, Y., Calderone, R., Fonzi, W., Liu, W., & Li, D. (2015) · Cellular Microbiology · doi:10.1111/cmi.12438 · Cited by 51 · see citing works
Guedouari, H., Gergondey, R., Bourdais, A., Vanparis, O., Bulteau, A. L., Camadro, J. M., & Auchère, F. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.07.006 · Cited by 45 · cited 1× · see citing works
“Proper mitochondrial distribution in the fila-ments could serve to power hyphal elongation, as hyphal growth depends more prominently on mitochondrial metabolism than does yeast growth (45).”
She, X., Zhang, L., Chen, H., Calderone, R., & Li, D. (2013) · Cellular Microbiology · doi:10.1111/cmi.12135 · Cited by 43 · cited 1× · see citing works
“Mitochondrial activity is needed for cell wall integrity in C. albicans (39–41; reviewed in references 5 and 6), and cell wall components, including 1,3-(cid:2) -glucan and cell wall mannosylation, correlate with inflammasome activation and pyroptosis (13, 19, 42–44).”
Verma‐Gaur, J., Qu, Y., Harrison, P. F., Lo, T. L., Quenault, T., Dagley, M. J., Belousoff, M. J., Powell, D., Beilharz, T. H., & Traven, A. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005590 · Cited by 33 · cited 1× · see citing works
“All primers used for quantitative RT-PCR are listed in Table S3 in the supplemental material, and some are further described in references 55 and 56.”
Hewitt, V. L., Heinz, E., Shingú-Vázquez, M., Qu, Y., Jeličić, B., Lo, T. L., Beilharz, T. H., Dumsday, G. J., Gabriel, K., Traven, A., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206345109 · Cited by 27 · cited 1× · see citing works
“Isolation of mitochondria and mitochondrial protein import assays were performed as previously described (54).”
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Kasper, L., König, A., Koenig, P.-A., Gresnigt, M. S., Westman, J., Drummond, R. A., Lionakis, M. S., Groß, O., Ruland, J., Naglik, J. R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06607-1 · Cited by 297 · see citing works
Tucey, T. M., Verma, J., Harrison, P. F., Snelgrove, S. L., Lo, T. L., Scherer, A. K., Barugahare, A. A., Powell, D., Wheeler, R. T., Hickey, M. J., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.03.019 · Cited by 228 · see citing works
“The detailed live cell imaging procedure is described in Tucey et al. (2016).”
BackgroundMethodCorcoran, S. E., Halai, R., & Cooper, M. A. (2021) · Pharmacological Reviews · doi:10.1124/pharmrev.120.000171 · Cited by 179 · see citing works
“albicans infection, leading the authors to propose that NLRP3 modulation during infection may be a therapeutic avenue to exploit (Tucey et al., 2016).”
BackgroundGut microbiota exaggerates triclosan-induced liver injury via gut-liver axis
Zhang, P., Zheng, L., Duan, Y., Gao, Y., Gao, H., Mao, D., & Luo, Y. (2021) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2021.126707 · Cited by 174 · see citing works
McGovern, B., Ford, C. B., Henn, M. R., Pardi, D. S., Khanna, S., Hohmann, E. L., O’Brien, E. J., Desjardins, C. A., Bernardo, P., Wortman, J. R., et al. (2020) · Clinical Infectious Diseases · doi:10.1093/cid/ciaa387 · Cited by 158 · see citing works
Molecular biology of coronaviruses: current knowledge
Artika, I. M., Dewantari, A. K., & Wiyatno, A. (2020) · Heliyon · doi:10.1016/j.heliyon.2020.e04743 · Cited by 116 · see citing works
The interplay between diet, gut microbes, and host epigenetics in health and disease
Shock, T., Badang, L., Ferguson, B. S., & Martinez, K. (2021) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2021.108631 · Cited by 101 · see citing works
Anti-Immune Strategies of Pathogenic Fungi
Marcos, C. M., de Oliveira, H. C., Melo, W., da Silva, J. D. F., Assato, P. A., Scorzoni, L., Rossi, S. A., Silva, A. C. A. D. P. E., Mendes‐Giannini, M. J. S., & Fusco‐Almeida, A. M. (2016) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2016.00142 · Cited by 94 · see citing works
Olivier, F. A. B., Hilsenstein, V., Weerasinghe, H., Weir, A. L., Hughes, S. A., Crawford, S., Vince, J. E., Hickey, M. J., & Traven, A. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111374 · Cited by 79 · see citing works
Verma, S., Shakya, V. P. S., & Idnurm, A. (2018) · Virulence · doi:10.1080/21505594.2017.1414133 · Cited by 67 · see citing works
“lysis and hence changing the outcome of the infection [127].”
BackgroundInfluentialO’Meara, T. R., Duah, K., Guo, C. X., Maxson, M. E., Gaudet, R. G., Koselny, K., Wellington, M. A., Powers, M. E., MacAlpine, J., O’Meara, M. J., et al. (2018) · mBio · doi:10.1128/mbio.01581-18 · Cited by 67 · see citing works
“pyroptosis (10, 27, 28), and we demonstrated that, upon phagocytosis, C.”
BackgroundBragazzi, N. L., Gianfredi, V., Villarini, M., Rosselli, R., Nasr, A., Hussein, A., Martini, M., & Behzadifar, M. (2018) · Frontiers in Public Health · doi:10.3389/fpubh.2018.00062 · Cited by 67 · see citing works
Protection of MCC950 against Alzheimer's disease via inhibiting neuronal pyroptosis in SAMP8 mice
Li, J., Zhuang, L., Luo, X., Liang, J., Sun, E., & He, Y. (2020) · Experimental Brain Research · doi:10.1007/s00221-020-05916-6 · Cited by 66 · see citing works
Secondary bile acids inhibit Candida albicans growth and morphogenesis
Guinan, J., Villa, P., & Thangamani, S. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty038 · Cited by 59 · see citing works
Koselny, K., Mutlu, N., Minard, A. Y., Kumar, A., Krysan, D. J., & Wellington, M. A. (2018) · mBio · doi:10.1128/mbio.01204-18 · Cited by 60 · see citing works
“in vitro (16): initial pyroptosis followed by nonpyroptotic cell death.”
BackgroundBai, X., Fu, R., Duan, Z., Liu, Y., Zhu, C., & Fan, D. (2021) · Food & Function · doi:10.1039/d1fo00242b · Cited by 56 · see citing works
Black, B., Lee, C., Horianopoulos, L. C., Jung, W. H., & Kronstad, J. W. (2021) · PLOS Pathogens · doi:10.1371/journal.ppat.1009661 · Cited by 51 · see citing works
Unique, Diverged, and Conserved Mitochondrial Functions Influencing Candida albicans Respiration
Sun, N., Parrish, R. S., Calderone, R. A., & Fonzi, W. A. (2019) · mBio · doi:10.1128/mbio.00300-19 · Cited by 51 · see citing works
“17), and biofilm formation (18), as well as interactions with neutrophils (19) and macrophages (20).”
Koch, B., Barugahare, A. A., Lo, T. L., Huang, C., Schittenhelm, R. B., Powell, D. R., Beilharz, T. H., & Traven, A. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.10.080 · Cited by 50 · see citing works
Weerasinghe, H., Simm, C., Djajawi, T. M., Tedja, I., Lo, T. L., Simpson, D. S., Shasha, D., Mizrahi, N., Olivier, F. A. B., Speir, M., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112522 · Cited by 47 · see citing works
König, A., Hube, B., & Kasper, L. (2020) · Toxins · doi:10.3390/toxins12080469 · Cited by 49 · see citing works
Metabolic competition between host and pathogen dictates inflammasome responses to fungal infection
Tucey, T. M., Verma, J., Olivier, F. A. B., Lo, T. L., Robertson, A. A. B., Naderer, T., & Traven, A. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008695 · Cited by 46 · see citing works
Innate Immune and Fungal Model of Alzheimer’s Disease
Parady, B. (2018) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-180073 · Cited by 39 · see citing works
Simm, C., Weerasinghe, H., Thomas, D. R., Harrison, P. F., Newton, H. J., Beilharz, T. H., & Traven, A. (2022) · Microbiology Spectrum · doi:10.1128/spectrum.00100-22 · Cited by 38 · see citing works
“BMDMs were stained with 1 mM CellTrackerGreen CFMDA dye (ThermoFischer C7025) in serum-free BMDM medium as described previously (71).”
MethodCairns, T. C., Feurstein, C., Zheng, X., Zhang, L. H., Zheng, P., Sun, J., & Meyer, V. (2019) · Fungal Biology and Biotechnology · doi:10.1186/s40694-019-0081-x · Cited by 32 · see citing works
Wang, Q., Verma, J., Vidan, N., Wang, Y., Tucey, T. M., Lo, T. L., Harrison, P. F., See, M., Swaminathan, A., Kuchler, K., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107528 · Cited by 31 · see citing works
The ERMES (Endoplasmic Reticulum and Mitochondria Encounter Structures) mediated functions in fungi
Kundu, D., & Pasrija, R. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.02.010 · Cited by 30 · see citing works
Geißel, B., Penka, M., Neubauer, M., & Wagener, J. (2017) · International Journal of Medical Microbiology · doi:10.1016/j.ijmm.2016.11.005 · Cited by 27 · see citing works
A mitochondrial proteomics view of complex I deficiency in Candida albicans
She, X., Zhang, P., Gao, Y., Zhang, L., Wang, Q., Chen, H., Calderone, R., Liu, W., & Li, D. (2018) · Mitochondrion · doi:10.1016/j.mito.2017.08.003 · Cited by 26 · see citing works
Druggable targets from coronaviruses for designing new antiviral drugs
Silva, L. R., Santos-Júnior, P. F. D. S., Brandão, J. D. A., Anderson, L., Bassi, Ê. J., de Araújo‐Júnior, J. X., Cardoso, S. H., & da Silva‐Júnior, E. F. (2020) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2020.115745 · Cited by 25 · see citing works
Guinan, J., & Thangamani, S. (2018) · FEMS Microbiology Letters · doi:10.1093/femsle/fny196 · Cited by 23 · see citing works
Koch, B., Tucey, T. M., Lo, T. L., Novakovic, S., Boag, P., & Traven, A. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02555 · Cited by 21 · see citing works
“…in filamentation on a solid substrate (i.e., plates), and a very similar mitochondrial morphology defect in hyphal cells of the gem11/1 mutant (Figure 5C) and themmm1 mutant (Tucey et al., 2016), we wondered whether, similarly to Gem1, ERMES is also needed for filamentation on solid substrates.”
BackgroundMethodInfluentialSelf-citationWeerasinghe, H., Stölting, H., Rose, A. J., & Traven, A. (2024) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00171-22 · Cited by 26 · see citing works
“Mitochondria are required for normal growth of C. albicans in both budding yeast morphology and invasive hyphal morphology, and hyphae are important for growing within macrophages and escaping from them in a rapid fashion (95, 96).”
Challagundla, N., Saha, B., & Agrawal-Rajput, R. (2022) · Immunologic Research · doi:10.1007/s12026-022-09286-9 · Cited by 22 · see citing works
“The hyphal growth determines the rate of inflammasome activation and inflammasome-mediated pyroptotic cell death [77, 131].”
BackgroundGenetic analysis of human and swine influenza A viruses isolated in Northern Italy during 2010–2015
Chiapponi, C., Ebranati, E., Pariani, E., Faccini, S., Luppi, A., Baioni, L., Manfredi, R., Carta, V., Merenda, M., Affanni, P., et al. (2017) · Zoonoses and Public Health · doi:10.1111/zph.12378 · Cited by 21 · see citing works
Paracoccidioidomycosis infection in domestic and wild mammals by Paracoccidioides lutzii
Mendes, J. F., Klafke, G. B., Albano, A. P. N., Cabana, Â. L., Teles, A. J., Camargo, Z. P. D., Xavier, M. O., & Meireles, M. C. A. (2017) · Mycoses · doi:10.1111/myc.12608 · Cited by 21 · see citing works
Interorganellar communication and membrane contact sites in protozoan parasites
Santos, H. J., & Nozaki, T. (2021) · Parasitology International · doi:10.1016/j.parint.2021.102372 · Cited by 20 · see citing works
Mitochondrial Control of Fungal Cell Walls: Models and Relevance in Fungal Pathogens
Koch, B., & Traven, A. (2019) · Current Topics in Microbiology and Immunology · doi:10.1007/82_2019_183 · Cited by 19 · see citing works
Song, J., Li, Y., Zhang, Z., Gao, X., Li, S., Zhang, J., Zhou, M., & Duan, Y. (2024) · Microbiological Research · doi:10.1016/j.micres.2024.127892 · Cited by 18 · see citing works
Balachandra, V. K., Verma, J., Shankar, M., Tucey, T. M., Traven, A., Schittenhelm, R. B., & Ghosh, S. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1009071 · Cited by 18 · see citing works
Kalindamar, S., Abdelhamed, H., Kordon, A. O., Pinchuk, L. M., & Karsi, A. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.681609 · Cited by 13 · see citing works
Neira, V., Allerson, M. W., Corzo, C. A., Culhane, M. R., Rendahl, A., & Torremorell, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0197600 · Cited by 13 · see citing works
Okamoto, M., Nakano, K., Takahashi-Nakaguchi, A., Sasamoto, K., Yamaguchi, M., Teixeira, M. C., & Chibana, H. (2023) · Journal of Fungi · doi:10.3390/jof9020240 · Cited by 11 · see citing works
“albicans, the ERMES complex is involved in immune system evasion [35] and cell wall stress responses [34].”
BackgroundAlonso, V. L., Carloni, M. E., Gonçalves, C. S., Peralta, G. M., Chesta, M. E., Pezza, A., Tavernelli, L. E., Motta, M. C. M., & Serra, E. C. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.642271 · Cited by 11 · see citing works
Role of Bile in Infectious Disease: the Gall of 7α-Dehydroxylating Gut Bacteria
Savidge, T., & Sorg, J. A. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2018.12.010 · Cited by 11 · see citing works
Influenza A virus vaccine research conducted in swine from 1990 to May 2018: A scoping review
Keay, S., Poljak, Z., Klapwyk, M., O'Connor, A. M. C., Friendship, R. M., O’Sullivan, T. L., & Sargeant, J. M. (2020) · PLoS ONE · doi:10.1371/journal.pone.0236062 · Cited by 9 · see citing works
Macrophage pyroptosis induced by Candida albicans
Zhang, F.-Y., Lian, N., & Li, M. (2024) · Pathogens and Disease · doi:10.1093/femspd/ftae003 · Cited by 10 · see citing works
“After 10 hours, the ASC a ggr egation no longer incr eased (Tucey et al. 2016 ).”
BackgroundCharacterization of mitogenomes from four Mucorales species and insights into pathogenicity
Liang, G., Zhang, M., Xu, W., Wang, X., Zheng, H., Mei, H., & Liu, W. (2021) · Mycoses · doi:10.1111/myc.13374 · Cited by 6 · see citing works
Bacterial Adherence to Plant and Animal Surfaces via Adhesin-Lipid Interactions
Rossi, C., Cazzola, H., Holden, N., & Rossez, Y. (2019) · Health Consequences of Microbial Interactions with Hydrocarbons, Oils, and Lipids · doi:10.1007/978-3-319-72473-7_13-1 · Cited by 7 · see citing works
Systems biology of host-Candida interactions: understanding how we shape each other
Hodgins-Davis, A., & O’Meara, T. R. (2020) · Current Opinion in Microbiology · doi:10.1016/j.mib.2020.04.001 · Cited by 5 · see citing works
Figueira, L. W., de Oliveira, J. R., NETTO, A. A. L., Zamarioli, L. D. S., Marcucci, M. C., Camargo, S. E. A., & de Oliveira, L. D. (2020) · Future Microbiology · doi:10.2217/fmb-2019-0297 · Cited by 5 · see citing works
An analysis of respiratory function and mitochondrial morphology in Candida albicansPreprint
Duvenage, L., Pentland, D. R., Munro, C. A., & Gourlay, C. W. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/697516 · Cited by 5 · see citing works
“In recent years, much of the machinery governing fission and fusion has been elucidated (Pagliuso, Cossart and Stavru 2018), including important contributors such as interaction with the ER (Tucey et al. 2016).”
BackgroundYang, G., Niu, X., Zhuang, T., Zhu, X., Xu, Q., Wang, H., Shao, J., Wang, C., Yang, Y., Wang, T., et al. (2025) · Virulence · doi:10.1080/21505594.2025.2519149 · Cited by 4 · see citing works
“A specific example is ERMES, a tether connecting the endoplasmic reticulum and mitochondria, which plays a role in evading the immune system by modulating inflammasome responses to hyphal signals in C. albicans [30].”
Inhibiting Inflammasomes with Small Molecules
Robertson, A. A. B. (2018) · Experientia supplementum · doi:10.1007/978-3-319-89390-7_15 · Cited by 4 · see citing works
Kumari, D., Kumar, M., Gaur, N. A., Duhan, L., Павловна, С. Н., Manoharlal, R., & Pasrija, R. (2025) · Journal of Cell Science · doi:10.1242/jcs.263558 · Cited by 3 · see citing works
Alvin, J. W., & Lacy, D. B. (2016) · Springer eBooks · doi:10.1007/978-94-007-6725-6_26-1 · Cited by 1 · see citing works
Zhou, Z., Wang, H., Liu, J., Yao, J., Zhang, J., Hou, R., Shim, W., Xiao, D., & Yi, T. (2025) · Virulence · doi:10.1080/21505594.2025.2555419
“Likewise, Mmm34, Mdm12, and Mdm1 mutations also exhibited obvious defects in the mitochondrial structure [18,35,36].”
Structure Function Studies of Large Clostridial Cytotoxins
Alvin, J. W., & Lacy, D. B. (2017) · Toxinology · doi:10.1007/978-94-007-6725-6_26-2
In silico analysis of coevolution among ERMES proteins, Pex11, and Lam6
Court, D. A., Khetoo, S., Shuvo, S. R., Reitmeier, S. D., & Hausner, G. (2017) · Canadian Journal of Microbiology · doi:10.1139/cjm-2017-0460
Role of Mitochondria in Fungal Drug Resistance
Pasrija, R., & Kundu, D. (2019) · Springer eBooks · doi:10.1007/978-981-32-9449-3_8
Reyes-Correa, A. J., Hernández-Flórez, N., Hernández-Espinosa, C. J., & García-Ayala, E. (2021) · Revista Española de Patología · doi:10.1016/j.patol.2021.04.001
The structural organization and functions of the ERMES complex in fungi
Wei, W., Zheng, B., & Fu, C. (2021) · Scientia Sinica Vitae · doi:10.1360/ssv-2021-0141
Gow, N. A. R., & Yadav, B. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.733159930.793545575
Hube, B., & Gresnigt, M. S. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.738437887.793577404
Weerasinghe, H., Simm, C., Djajawi, T. M., Tedja, I., Lo, T. L., Shasha, D., Mizrahi, N., Olivier, F. A. B., Speir, M., Lawlor, K. E., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.28.529319
“Bone marrow containing monocytes was flushed from these bones using BMDM media (RPMI 1640 supplemented with 12.5 mM HEPES, 10% FBS, 20% L-cell conditioned medium and 100U/ ml of penicillin-streptomycin) and allowed to differentiate into BMDMs for 5-7 days as previously described(Tucey et al., 2016).”
MethodInfluentialER-mitochondrial crosstalk (ERMES) regulates cell wall composition in pathogenic fungi
Kumari, D., Bari, V. K., & Pasrija, R. (2025) · Archives of Microbiology · doi:10.1007/s00203-025-04448-3
“Similarly, C. albicans ERMES mutants form shorter hyphae and do not undergo invasive filament formation (Tucey et al. 2016; Koch et al. 2017 ).”
Influential
- Authors
- Tucey, T. M., Verma-Gaur, J., Nguyen, J., Hewitt, V. L., Lo, T. L., Shingu-Vazquez, M., Robertson, A. A. B., Hill, J. R., Pettolino, F. A., Beddoe, T., Cooper, M. A., Naderer, T., & Traven, A.
- Affiliations
- Monash University (AU)
- Infection and Immunity Program and the Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria, Australia
- The University of Queensland (AU)
- Commonwealth Scientific and Industrial Research Organisation (AU)
- La Trobe University (AU)
- Corresponding author
- Traven, Ana
- ORCID
- Venue
- mSphere
- Publisher
- American Society for Microbiology
- Published
- 2016-06-22
- Volume
- 1
- Issue
- 3
- ISSN
- 2379-5042 (ISSN-L)
- PMC
- PMC4888881
- OpenAlex
- W2398372682
- Cited by
- 66
- References
- 58
- Citations by year
- 2025: 4 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 12 · 2020: 12 · 2019: 7 · 2018: 12 · 2017: 7 · 2016: 3
- FWCI
- 5.03
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- mSphere (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Monash University Research Portal (Monash University) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- La Trobe University (cc-by)
- Funders
- Department of Health | National Health and Medical Research Council (APP1023973, APP1081072, APP1101562)
- Australian Research Council (DE140101164)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- ERMES, Candida albicans, NLRP3 inflammasome, pyroptosis, macrophage escape, hyphal elongation, β-1,3-glucan, cell wall remodeling, MCC950, caspase-1, antifungal drug targets
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