Pathogenic fungi are a significant burden to public health, recently estimated to cause 2.5 million annually attributable deaths worldwide (Denning, 2024). Among these, Candida species are responsible for more than 100 million mucosal infections and 1.5 million systemic infections, representing the fourth most frequent cause of bloodstream infection in hospitalized patients (Denning, 2024; Brown et al., 2012; Sharma and Chakrabarti, 2023). Candida albicans is the most common opportunistic species, which in healthy individuals often colonizes mucosal surfaces (oral cavity, gastrointestinal tract, as well as genital tract) (d’Enfert et al., 2021), but leads to invasive infection, post trauma or when immune system of the host is compromised. C. albicans is classified in the critical priority group of the WHO list of fungal pathogens (WHO, 2022).

Fungal cells are enveloped by a cell wall, which is essential for protection, integrity, and to maintain cell morphology. During commensalism with human hosts, the cell wall enables fungi to survive host defenses, whereas during pathogenic interactions the cell wall also plays a central role in the polarized growth of invasive hyphae, thereby facilitating host tissue invasion (Hall, 2015; Mishra et al., 2022). The cell wall architecture is dynamic and therefore critical in modulating the host immune responses (Brown, 2011; Netea et al., 2015), which are driven by host immune receptors (pattern recognition receptors [PRRs]) (Netea et al., 2006; Erwig and Gow, 2016; Dambuza et al., 2017). Recognition of fungal pathogen-associated molecular patterns (PAMPs) by host PRRs triggers an array of antifungal responses, including phagocytosis, the production of reactive oxygen/nitrogen species (ROS/RNS), neutrophil extracellular traps, and the release of cytokines and chemokines that recruit immune cells to the site of infection and activate adaptive immunity (Dambuza et al., 2017; Lionakis and Levitz, 2018; Urban et al., 2006; Gow et al., 2011). Being extracellular, thereby first to interact with the host immune system, fungal cell wall components function as the major PAMPs.

The cell wall of C. albicans is a complex structure with a fibrillar outer layer of mannoproteins and an inner polysaccharide layer composed of chitin, β-1,3-glucan and β-1,6-glucan, which are not present in mammalian cells (Gow and Hube, 2012). Dectin-1, a C-type lectin receptor that recognizes fungal cell wall β-1,3-glucan, has been demonstrated to play a dominant pro-inflammatory role in antifungal immunity (Brown et al., 2002; Brown and Gordon, 2003; Taylor et al., 2007; Ferwerda et al., 2009; Marakalala et al., 2013). Chitin particles derived from the C. albicans cell wall lead to the selective secretion of the anti-inflammatory cytokine IL-10 (Wagener et al., 2014). Mannans from C. albicans are recognized by multiple receptors expressed on different immune cells (Mannose receptor, DC-SIGN, TLR4, Dectin-2, Dectin-3), which are involved in yeast phagocytosis and appear to play a critical role in the induction of Th17 responses (Hall and Gow, 2013; Choudhury et al., 2023). C. albicans has developed strategies to sense environmental signals encountered within the host and to regulate the exposure of its cell wall PAMPs. For example, low levels of β-1,3-glucan exposure by C. albicans correlate with enhanced colonization of the gastrointestinal tract (Sem et al., 2016; Hopke et al., 2018) and β-1,3-glucan is mainly hidden from immune recognition by the outer layer of mannan fibrils (Erwig and Gow, 2016; Lenardon et al., 2020; Graus et al., 2018). Although these C. albicans cell wall polysaccharide PAMPs have been investigated in the context of host–fungal interaction, the immunomodulatory potentials of β-1,6-glucan, another major constituent of the C. albicans cell wall, remains under-investigated.

The composition and organization of the fungal cell wall result from an equilibrium between syntheses and remodeling of the constituent polysaccharides (Hall and Gow, 2013; Gow et al., 2017). β-Glucans and chitin, which account for about 60% and 2–10% (depending on the morphotype), respectively, are cross-linked to form the skeletal armor of the C. albicans cell wall (Gow et al., 2011; Klis et al., 2009). Mannoproteins, which are predominantly glycosylphosphatidylinositol (GPI)-modified and covalently linked to the skeletal polysaccharides via β-1,6-glucan bridges (Klis et al., 2009; Liu et al., 2016), account for 30–40% of the cell wall. β-1,6-Glucan is composed of a linear chain of β-1,6-linked glucose residues with few short side chains of β-1,3-glucoside or laminaribioside residues (Iorio et al., 2008; Aimanianda et al., 2009). According to analytical methods, the β-1,6-glucan content is highly variable, from 15 to 50% (Mio et al., 1997; Herrero et al., 2004; Free, 2013; Schiavone et al., 2014). Although β-1,6-glucan plays a crucial structural role in the C. albicans cell wall, the dynamics of this cell wall polysaccharide as a function of growth or stress conditions remains underexplored.

Genes required for the full β-1,6-glucan production have been identified in model yeast, Saccharomyces cerevisiae (Brown et al., 1993). Among them, KRE5 codes a putative α-glucosyltransferase (CAZy, 2024a) (GT-24) localized in the endoplasmic reticulum (ER); its deletion results in the absence of β-1,6-glucan in S. cerevisiae and about 80% reduction in cell wall β-1,6-glucan content in C. albicans (Herrero et al., 2004; Levinson et al., 2002). Functions of Kre1, Kre6, Kre9 and the related homologs are unclear. Their localization in the ER, Golgi, plasma membrane, or extracellular culture medium suggests an intracellularly initiating biosynthetic pathway of β-1,6-glucan (Lesage and Bussey, 2006; Montijn et al., 1999). KRE6 and its functional homolog SKN1 share 66% identity and both encode transmembrane proteins containing a glycosyl-hydrolase domain (GH-16). KRE6 deletion in S. cerevisiae results in a 70% decrease in the cell wall β-1,6-glucan content (Aimanianda et al., 2009). In C. albicans, the double deletion of KRE6 and SKN1 leads to a slow growth, cell wall abnormalities, cell separation failure, and reduced virulence (Han et al., 2019a; Han et al., 2019b). Two more KRE6 homologs (KRE62 and SKN2) have been identified in C. albicans (CGD, 2024) but their function has not yet been investigated, and the C. albicans cell wall β-1,6-glucan biosynthetic pathway, namely the β-1,6-glucosyltransferase involved in β-1,6-glucan polymerization and other enzymes involved in β-1,6-glucan remodeling (elongation, branching, or cross-linking with β-1,3-glucan), remains to be identified.

We standardized biochemical approaches to quantify as well as to characterize β-1,6-glucan of C. albicans, which allowed us to perform comparative analysis and to study the dynamic of this cell wall polysaccharide in response to stress conditions and to antifungal treatments. β-1,6-Glucan biosynthesis appears to be a compensatory reaction when mannan elongation is defective, whereas the absence of β-1,6-glucan results in a significantly sick growth phenotype and complete cell wall reorganization. Moreover, β-1,6-glucan showed a distinct immunomodulatory response compared to other cell wall polysaccharides. Together, our study establishes overarching and critical roles for β-1,6-glucans in the organization, structure, biosynthesis, and immunomodulatory properties of the cell wall.

Cell wall β-1,6-glucan is a conserved constituent in most of the major human fungal pathogens, including Candida, Cryptococcus, Pneumocystis, Histoplasma, and Malassezia species (Garcia-Rubio et al., 2020; Stalhberger et al., 2014; Kottom et al., 2015). The cell wall of fungal pathogens is the target of several classes of antifungal drugs and is critical for immune recognition and activation, and therefore has been the subject of numerous investigations (Gow et al., 2017; Garcia-Rubio et al., 2020). However, this polysaccharide has been neglected, perhaps because its analysis requires bespoke methodologies. Here, we established new biochemical tools for quantitative and comparative analysis of cell wall β-1,6-glucan dynamics and structure in C. albicans and used them to demonstrate that this polysaccharide is instrumental in determining the gross architecture of the fungal wall and its immune reactivity.

In SD medium at 37°C, β-1,6-glucan represents 23% of the total cell wall, with an average size of 58 kDa (Figure 1). From our analytical data on C. albicans cell wall, we proposed an updated model underlining the true role of β-1,6-glucan as a major cell wall component (Figure 7a). NMR has demonstrated that the structure of β-1,6-glucan in the yeast cell wall is similar between species (Aimanianda et al., 2009; Stalhberger et al., 2014), but there are variations in β-1,6-glucan content, chain length, and branching. Malassezia restricta contains long β-1,6-glucan chains, averaging 80 kDa, whilst in S. cerevisiae and C. albicans they are moderate in size (30–60 kDa). We showed here that modulating environmental conditions induce significant changes in both cell wall structure and content. As described previously, lactate used as the sole carbon source led to a thinner inner cell wall layer and greater exposure of β-1,3-glucan (Ene et al., 2012; Ballou et al., 2016). We observe here that lactate medium also led to a marked reduction in cell wall β-1,6-glucan content and chain length (Figure 2, Figure 7b). Our data showed that several factors related to host niches (morphology, temperature, salinity, pH, and presence of organic acids) and the presence of antifungals had a significant impact on the structure, size, and branching of β-1,6-glucan (Figure 7b). This dynamic nature of the β-1,6-glucan component of the wall (Figure 2, Figure 2—figure supplement 1, Figure 3—figure supplement 1) is as important as the regulation and structural diversity of chitin, mannan, and β-1,3-glucan (Gow and Lenardon, 2023).

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The dynamic regulation of mannan biosynthesis leading to structural changes in the outer mannoprotein layer of C. albicans is also under-investigated. C. albicans evolves in different environments as a commensal or pathogen (d’Enfert et al., 2021), mainly in the gut, oral cavity, genital tract, and blood. How fungal cell walls adapt to changing environments was recently been listed as one of the top five unanswered question in fungal cell surface research (Gow et al., 2023). Our data demonstrate that in response to several environmental factors β-1,6-glucan and mannan productions are coupled. The in vivo importance of this novel dynamic process remains to be addressed but it could be critical in the articulation of host inflammatory responses (de Assis et al., 2022; Chen et al., 2022).

Immunolabeling with an anti-β-1,6-glucan serum demonstrated that this polymer is exposed at the cell surface and is therefore accessible to receptors that stimulate human immune cells (Figure 6—figure supplement 5, Figure 6). Similarly in Pneumocystis carinii, β-1,6-glucans are exposed to the cell surface and stimulate mouse macrophages, leading to the release of TNF-α (Kottom et al., 2015). Our immunological data indicate that β-1,6-glucan is a bona fide fungal cell wall PAMP that activates the human immune system (Figure 7d). Beads coated with pustulan (an insoluble linear form of β-1,6-glucan) activate neutrophils and induce massive ROS production and phagocytosis in a dectin-1-independent manner (Rubin-Bejerano et al., 2007; Palma et al., 2006). We observed that the absence of human serum in the culture medium led to a strong reduction in β-1,6-glucan-induced cytokine secretion from PBMCs and that β-1,6-glucan bind to C3b (Figure 6—figure supplement 4). These data are in agreement with the binding of pustulan to C3b/C3d, as described previously (Rubin-Bejerano et al., 2007; Palma et al., 2006). This allows us to assume that the opsonization by complement component C3 could partially mediate the recognition of β-1,6-glucan by immune cells, but needs to be validated experimentally. We observed that the size of soluble β-1,6-glucan did not alter immune stimulation in vitro (Figure 6—figure supplement 1), whereas, despite its ability to bind soluble and particulate β-1,3-glucan polymers, Dectin-1 signaling is only activated by particulate β-1,3-glucans (Goodridge et al., 2011). The relevance of fungal β-1,6-glucan to the global host immune response and mechanism of recognition remains to be investigated.

In C. albicans, β-1,3-glucan exposure is regulated by external signals such as hypoxia, carbon source, or iron deprivation via the upregulation of β-1,3-glucanase activities that lead to β-1,3-glucan masking and immune evasion (de Assis et al., 2022; Childers et al., 2020b; Yang et al., 2022). Regulation of the mechanisms determining β-1,6-glucan exposure and the expression of secreted glucanases remain also unknown in C. albicans. The absence of β-1,6-glucan in the AI fraction led to a reduced inflammatory response (Figure 6), suggesting that an endo-β-1,3-glucanase, such as Eng1, may enable the release of cross-linked β-1,6-glucan from the cell surface, which could attenuate the host response by pruning β-1,6-glucans that are covalently bound to β-1,3-glucans from the surface (Yang et al., 2022).

Cell wall organization in C. albicans depends on the cross-linking of all polymers that function as a dynamic flexible network (Gow et al., 2017; Garcia-Rubio et al., 2020). Their interconnectedness means that alteration in the synthesis of one polymer can lead to a compensatory change and cell wall remodeling. Our data provides one new example of this phenomenon, namely decrease in cell wall chitin content results in an increase in both β-1,3-glucans and β-1,6-glucans in the AS fraction of the wall. Chitin exists in the yeast cell wall in three forms: free (~40%), and cross-linked to β-1,3-glucan (40–45%) or β-1,6-glucan (15–20%) and cross-linked β-glucan-chitin forms the core fibrillar cell wall structure resistant to alkali solubilization (Gow et al., 2017; Cabib, 2009; Cabib and Durán, 2005; Cabib et al., 2007). Therefore, a decrease in the chitin content might reduce the formation of fibrillar structure, thereby releasing the β-glucan contents into the AS fraction. On the other hand, in the FKS1 mutant or upon caspofungin treatment, cell wall chitin and β-glucan-chitin contents were increased, which could be attributed to an upregulated CRH1 expression due to decreased β-1,3-glucan synthesis as in FKS1 mutant (Terashima et al., 2000) or due to caspofungin treatment. CRH family members are involved in the β-glucan-chitin cross-linking (Cabib, 2009). Interestingly, defects in the expression of CHS1 that encodes an essential chitin synthase required to construct the primary septum were also compensated by an increased content of cell wall β-1,6-glucan but not of β-1,3-glucan (Figure 3). This suggests that Chs1 has other functions beyond septum construction that had previously been suggested by loss of cell integrity and swelling of cells upon CHS1 repression (Munro et al., 2001). In S. cerevisiae, deletion of GAS1, the ortholog of PHR1 and PHR2, led to a strong decrease in cross-linked β-1,6-glucan to β-1,3-glucan-chitin cell wall core (Aimanianda et al., 2017). Deletions of PHR1 and PHR2, holding a β-1,3-glucan remodeling activity, led to an increased chitin content (Figure 3—figure supplement 1) and a reduction in β-1,3-glucan branching (Figure 3—figure supplement 2). However, a decrease in β-1,6-glucan content and β-1,6-glucan size was only observed in the PHR2 mutant (Figure 3). As PHR1 and PHR2 genes are strongly regulated by external pH, the compensatory differences we described may be explained by pH-dependent regulation of β-1,6-glucan synthesis (Figure 3).

In C. albicans, the mannan moieties of glycoproteins are covalently cross-linked to the β-glucan-chitin core. Mutants defective in N-mannan elongation led to a marked increase in β-1,6-glucan content and size (Figure 3). In yeast, Och1 and Mnn9 are α-1,6-mannosyltransferases that are involved in initial steps of α-1,6-mannan polymerization in the Golgi. Members of the Mnn2 α-1,2 mannosyltransferases are required for the addition of the side chains of the α-1,6-mannan backbone (Hall and Gow, 2013). Mutants in these genes led to defects in the outer fibrillar layer (Lenardon et al., 2020; Southard et al., 1999) and increased β-1,3-glucan exposure (Hall and Gow, 2013; Yadav et al., 2020). The quantification of β-1,6-glucan content in these N-mannan-deficient mutants had not been described previously in C. albicans (Hall and Gow, 2013; Southard et al., 1999) and underline the new finding that the regulation of mannan, β-glucans, and chitin synthesis is coordinated and coupled. Screening with K1 toxin killer revealed a hypersensitivity of the Scmnn9 mutant and an increase in β-1,6-glucan cell wall content (Pagé et al., 2003), reinforcing the hypothesis that β-1,6-glucans play a compensatory role when N-mannosylation is compromised (Figure 7c). Thus, a defect in the fibrillar outer mannan layer led to an increase in the inner cell wall chitin and β-1,6-glucan contents (Figure 3—figure supplement 1), suggesting that their synthesis was regulated by a rescue mechanism associated with the reprogramming of specific transcriptional responses via the cell wall integrity (CWI) pathway (Childers et al., 2020a). Defects in O-mannosylation also affected β-1,6-glucan synthesis, leading to shortened highly branched β-1,6-glucan chains, without significant changes in overall cell wall composition, suggesting a specific inhibition of the elongation of β-1,6-glucan chain and showing that size and branching of β-1,6-glucan can be regulated independently (Figure 7c).

Fine details of the biosynthetic pathway of yeast β-1,6-glucans are not clear. In S. cerevisiae, deletion of KRE5 and ROT2 led to a reduction in cell wall β-1,6-glucans (Shahinian and Bussey, 2000). In C. albicans, this reduction is characterized by the presence of short seldom-branched β-1,6-glucan chains (Figure 3). Although no difference was observed in the CWH41 mutant, our data imply that canonical N-glycan processing in the ER is required for complete β-1,6-glucan synthesis (Pagé et al., 2003), and that Kre5p is not the β-1,6-glucan polymerase (Herrero et al., 2004). Furthermore, our results confirm that the β-1,6-glucan biosynthetic pathway is similar in these phylogenetically distant yeasts, and that the N-glycosylation pathway is critical for β-1,6-glucan synthesis. Defects in early N-glycan synthesis at the ER level led to concomitant defects in β-1,6-glucan synthesis while defects in N-mannan elongation led to increased β-1,6-glucan synthesis. However, as Kre5, Rot2, and Cwh41 are part of the calnexin cycle involved in the control of N-glycoprotein folding in the ER, early N-glycan synthesis may have an indirect effect in ensuring the functionality of the enzymes rather than the synthesis of N-glycan moiety required for β-1,6-glucan synthesis. Our hypothesis is that this biosynthesis begins intracellularly. According to in vitro systems in S. cerevisiae, the initial step is the polymerization of a linear chain by a β-glucosyltransferase using UDP-glucose as the sugar donor (Aimanianda et al., 2009; Vink et al., 2004) and probably an as yet unknown acceptor (Figure 7—figure supplement 1). The second step would be the addition of glucoside and laminaribioside as a side chain. Finally, after release into the cell wall, β-1,6-glucan will be cross-linked to the other cell wall polymers. Among the KRE genes, only KRE6 may be directly involved in β-1,6-glucan synthesis. Kre6 and its homologs contain a β-glycosyl-hydrolase domain of the GH-16 family, which includes a large number of fungal enzymes such as Crh1 homologs that are involved in the cross-linking of chitin and β-1,3-glucan (Cabib, 2009). In C. albicans, the quadruple deletion of KRE6, SKN1, SKN2, and KRE62 led to the complete absence of β-1,6-glucan in the cell wall (Figures 3 and 7e) but also in culture supernatants and in intracellular extracts (not shown), demonstrating a stop of β-1,6-glucan synthesis rather than miss-localization. The absence of β-1,6-glucan in the quadruple mutant led to global cell wall remodeling and the absence of the outer fibrillar N-mannan layer (Figures 5 and 7e). Kre6 had the dominant role and its absence led to a hypersensitivity to cell wall-targeting antifungal drugs (Mio et al., 1997; Han et al., 2019b). One exception was observed for caspofungin, which enhanced the growth of all KRE6 deleted mutants (Figure 4c). Growth above the MIC (paradoxical growth) has been described at high caspofungin concentrations and is associated with high chitin content (Han et al., 2019a; Rueda et al., 2014) as observed in these mutants. Our data show that Kre6 is required for the production of normal amounts of β-1,6-glucan and that the remaining β-1,6-glucans present in kre6Δ/Δ was composed of short and highly branched chains. This suggests that the Kre6 family is required for the polymerization and/or elongation of β-1,6-glucan, but not glucan branching.

In S. cerevisiae, only two KRE6 family members have been identified, Kre6 and Skn1, and their absence led to strong growth defects and hypersensitivity to cell wall perturbing agents – similar to what we observed here in C. albicans (Roemer et al., 1993). In C. neoformans, among the six KRE6 homologs, KRE6 and SKN1 are required for the production of cell wall β-1,6-glucan (Gilbert et al., 2010), and although the KRE6 family is essential for β-1,6-glucan synthesis, its biochemical function remains unknown. Kre6 homologs are type II membrane proteins with a GH-16 domain at the luminal C-terminus and an unfolded cytosolic N-terminal tail (Kurita et al., 2011). Yeast Kre6 and Skn1 proteins have moderate similarity with diatom TGS (1,6-β-transglycosylase) proteins (Kroth et al., 2008; Huang et al., 2016) and can synthesize glucan from UDP-Glc (Inukai et al., 2023). Kre6 homologs share structural similarities with β-glucanases and β-transglycosylases, arguing for a possible cell wall remodeling function. In S. cerevisiae, Kre6p has been localized in the endoplasmic reticulum, the plasma membrane, and secretory vesicle-like compartments (Shahinian and Bussey, 2000; Kurita et al., 2011; Kurita et al., 2012), and the cytosol tail was shown to be essential for the correct cellular localization and β-1,6-glucan synthesis (Kurita et al., 2011). Surprisingly, in C. albicans the cytosol tail is not essential (Han et al., 2019b), suggesting some functional differences of this protein in these yeasts. In C. albicans, the double KRE6/SKN1 mutant is avirulent in a mice model of candidiasis (Han et al., 2019b), showing that the β-1,6-glucan biosynthetic pathway is a potential virulence target. However, the drugs jervine (steroidal alkaloid) and a pyridobenzimidazole derivate (D75-4590), which may target Kre6 and inhibit S. cerevisiae growth (Kubo et al., 2022; Kitamura et al., 2009), had no effect on C. albicans (Kubo et al., 2022; Kitamura et al., 2009), presumably representing species-specific differences in drug profiles. Kre6 family members are present in all fungal pathogens producing cell wall β-1,6-glucans, and further investigations are required to understand the enzyme activities and the diversity of structures related to the potential drug targeting of these proteins.

Overall, this work highlights the central role that β-1,6-glucan plays in orchestrating cell wall synthesis during growth and in response to stress and sets the focus for further work that can exploit this central role in mitigating fungal infections.

All data supporting the findings of this study are available as source data files linked to the corresponding figure or figure supplement.

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Author details

1. Clara Bekirian

   Institut Pasteur, Université Paris Cité, INRAE, USC2019, Unité Biologie et Pathogénicité Fongiques, Paris, France

   Contribution

   Conceptualization, Data curation, Formal analysis, Investigation, Methodology, Writing – original draft, Writing – review and editing

   Competing interests

   No competing interests declared

   "This ORCID iD identifies the author of this article:" 0009-0004-9300-949X

2. Isabel Valsecchi

   EA DYNAMYC 7380, Faculté de Santé, Université Paris-Est Créteil (UPEC), École Nationale Vétérinaire d'Alfort (EnvA), USC Anses, Créteil, France

   Contribution

   Formal analysis, Methodology

   Competing interests

   No competing interests declared

3. Sophie Bachellier-Bassi

   Institut Pasteur, Université Paris Cité, INRAE, USC2019, Unité Biologie et Pathogénicité Fongiques, Paris, France

   Contribution

   Conceptualization, Supervision, Methodology

   Competing interests

   No competing interests declared

4. Cyril Scandola

   Institut Pasteur, Université Paris Cité, Ultrastructural Bioimaging Unit, Paris, France

   Contribution

   Methodology

   Competing interests

   No competing interests declared

   "This ORCID iD identifies the author of this article:" 0000-0002-5305-9095

5. J Inaki Guijarro

   Institut Pasteur, Université Paris Cité, CNRS UMR3528, Biological NMR and HDX-MS Technological Platform, Paris, France

   Contribution

   Formal analysis, Visualization, Methodology, Writing – original draft

   Competing interests

   No competing interests declared

6. Murielle Chauvel

   Institut Pasteur, Université Paris Cité, INRAE, USC2019, Unité Biologie et Pathogénicité Fongiques, Paris, France

   Contribution

   Formal analysis, Methodology

   Competing interests

   No competing interests declared

7. Thierry Mourer

   Institut Pasteur, Advanced Molecular Virology Group, Paris, France

   Contribution

   Methodology

   Competing interests

   No competing interests declared

8. Neil AR Gow

   Medical Research Council Centre for Medical Mycology, University of Exeter, Exeter, United Kingdom

   Contribution

   Resources, Writing – original draft, Writing – review and editing

   Competing interests

   No competing interests declared

9. Vishu Kumar Aimanianda

   Institut Pasteur, Université Paris Cité, Immunobiology of Aspergillus Group, Paris, France

   Contribution

   Conceptualization, Resources, Formal analysis, Supervision, Validation, Methodology, Writing – original draft, Writing – review and editing

   Competing interests

   No competing interests declared

   "This ORCID iD identifies the author of this article:" 0000-0001-5813-7497

10. Christophe d'Enfert

    Institut Pasteur, Université Paris Cité, INRAE, USC2019, Unité Biologie et Pathogénicité Fongiques, Paris, France

    Contribution

    Resources, Validation, Writing – original draft, Project administration, Writing – review and editing

    Competing interests

    No competing interests declared

11. Thierry Fontaine

    Institut Pasteur, Université Paris Cité, INRAE, USC2019, Unité Biologie et Pathogénicité Fongiques, Paris, France

    Contribution

    Conceptualization, Resources, Data curation, Formal analysis, Supervision, Funding acquisition, Validation, Investigation, Visualization, Methodology, Writing – original draft, Project administration, Writing – review and editing

    For correspondence

    thierry.fontaine@pasteur.fr

    Competing interests

    No competing interests declared

    "This ORCID iD identifies the author of this article:" 0000-0002-8184-789X

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