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De Cock, H. Growth of Aspergillus fumigatus in Biofilms. Encyclopedia. Available online: https://encyclopedia.pub/entry/18779 (accessed on 18 December 2025).
De Cock H. Growth of Aspergillus fumigatus in Biofilms. Encyclopedia. Available at: https://encyclopedia.pub/entry/18779. Accessed December 18, 2025.
De Cock, Hans. "Growth of Aspergillus fumigatus in Biofilms" Encyclopedia, https://encyclopedia.pub/entry/18779 (accessed December 18, 2025).
De Cock, H. (2022, January 25). Growth of Aspergillus fumigatus in Biofilms. In Encyclopedia. https://encyclopedia.pub/entry/18779
De Cock, Hans. "Growth of Aspergillus fumigatus in Biofilms." Encyclopedia. Web. 25 January, 2022.
Growth of Aspergillus fumigatus in Biofilms
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This entry is adapted from the peer-reviewed paper 10.3390/jof8010048

Biofilm formation during infections with the opportunistic pathogen Aspergillus fumigatus can be very problematic in clinical settings, since it provides the fungal cells with a protective environment. Resistance against drug treatments, immune recognition as well as adaptation to the host environment allows fungal survival in the host. The exact molecular mechanisms behind most processes in the formation of biofilms are unclear. In general, the formation of biofilms can be categorized roughly in a few stages; adhesion, conidial germination and development of hyphae, biofilm maturation and cell dispersion. Fungi in biofilms can adapt to the in-host environment. These adaptations can occur on a level of phenotypic plasticity via gene regulation. However, also more substantial genetic changes of the genome can result in increased resistance and adaptation in the host, enhancing the survival chances of fungi in biofilms. Most research has focused on the development of biofilms. 

Aspergillus fumigatus biofilm in-host adaptation gene expression

1. Introduction

Aspergillus fumigatus (A. fumigatus) is a saprophytic fungus that can normally be found in the soil, where it lives on organic debris. The airborne conidia of this opportunistic fungus are spread abundantly, and hundreds of conidia are inhaled by humans on a daily basis [1]. Inhalation of these conidia by healthy individuals is normally not harmful since they are eliminated by lung innate immune defense systems like mucociliary clearance [2] and alveolar macrophages, the main phagocytic cells of the respiratory tract [3]. However, A. fumigatus can cause infections in the respiratory tract of immunocompromised individuals, such as patients following chemotherapy, receiving transplants and immune-suppressive drugs or those in intensive care [4][5]. In most of these patients, A. fumigatus infection starts in the respiratory tract, resulting in varying clinical diseases such as invasive aspergillosis (IA), allergic bronchopulmonary aspergillosis (ABPA) and aspergilloma [1]. Next to Candida albicans (C. albicans), A. fumigatus is also a major pathogen responsible for nosocomial infections. Whereas Candida species are responsible for 80% of fungal nosocomial infections [6], A. fumigatus is the most common species to occur in infections in the airways of immunocompromised individuals, causing severe and fatal invasive infections [1].
Developments in medical therapy and technology such as organ transplantations accompanied with immunosuppression and new chemotherapeutic agents have increased the survival of patients suffering from severe diseases that previously would be fatal. Due to these advances in medical technology, the number of immunocompromised patients that are vulnerable to nosocomial infections by fungi has also increased [7]. In hospitals, nosocomial aspergillosis has become a severe threat to immunosuppressed patients due to the airborne conidia of A. fumigatus, and where outbreaks of nosocomial aspergillosis can occur due to construction work or deficient ventilation systems [8][9]. Moreover, the implementation of medical devices such as prostheses, catheters, and mechanical heart devices are also a major source of fungal as well as bacterial infections that can be difficult to treat [10][11].
Infection of A. fumigatus can be severe and difficult to treat due to its ability to form a biofilm on surfaces [12]. These biofilms consist of a microbial community that can strongly adhere to each other and to biotic and abiotic surfaces. The microbial community is encased by a polymeric extracellular matrix (ECM), that is composed of primarily of polysaccharides. The ECM functions as a protective sheet and offers a framework for cell cohesion and adhesion to the surface [13]. Moreover, the ECM controls dispersion of cells and acts as a source of nutrients for the cells. The shield of biofilm also possesses defensive characteristics, making the biofilm more tolerant against immune cells and drug treatments [10].

2. Stages of Biofilm Development and Molecular Pathways

The formation of a fungal biofilm starts with the attachment of conidia to the biotic or abiotic surface. In vitro studies using scanning electron microscopy (SEM) and confocal laser scanning microscopy [14][15] showed that the formation of A. fumigatus biofilm can be roughly divided into different stages; (1) adhesion to the surface, (2) conidial germination into hyphae and development, (3) biofilm maturation with development of mycelia, ECM production, hyphal layering networks and formation of channels, and (4) cell dispersion [15]. In C. albicans, the stages of biofilm development are similar to A. fumigatus and comprise adhesion, initiation of biofilm formation, biofilm maturation and dispersion [16].

2.1. Adhesion

Adhesion is considered to be an important step in the process of fungal infection, since it is the first interaction between the fungi and the host. After inhalation, the airborne conidia come in contact with the respiratory tract and adhere onto airway epithelial cells [17]. The initial attraction between the conidia and surface is weak, and to strengthen attachment to the host surface, cell-surface components known as adhesins are used in fungal biofilm formation [15]. In the biofilm formation of C. albicans, fungal adhesion is regulated by members of a class of proteins known as glycosylphosphatidylinositol-dependent cell wall proteins (GPI-CWP). These GPI-CWP proteins include Hwp1, Hwp2 and a group of eight adhesion genes (ALS1-ALS7 and ALS9) that are part of the agglutinin-like sequence (ALS) family. These genes encode for proteins that possess characteristics of adhesin glycoproteins on the cell surface [18][19][20].
In A. fumigatus, electron microscopic and biochemical studies have identified molecules on the outer layer of the cell wall of A. fumigatus conidia. This study showed that the outer layer of the conidia was characterized by a layer of rodlets made of hydrophobins, a family of small hydrophobic proteins on the cell surface [21]. These hydrophobins were identified as RodAp, RodBp, RodCp, RodDp, RodEp and RodFp [15]. It is suggested that the hydrophobic characteristic of these proteins allows for their adhesion to hydrophobic abiotic or biotic surfaces, and that they are involved in the initiation of the biofilm process [22]. In a study where single and multiple hydrophobin-deletion mutants were constructed, the results showed that only RodA is necessary for efficient rodlet formation on the cell surface of conidia and adherence on polystyrene plates [23]. RodA proved to be responsible for hydrophobicity, integrity of the cell wall, conidial production, and susceptibility to external factors such as drugs. The importance of RodA was also observed in another study, where disruption of RodA decreased adherence of conidia to collagen and albumin, although not laminin or pulmonary epithelial cells [17]. The rodlet layer that includes RodA, also disguises the fungal cell wall components β-glucan, chitin, and glycoproteins that can provoke immunogenic reactions. Whereas β-glucan is recognized by receptors such as Dectin-1 in case of interaction of epithelial cells, interaction with ephrin type-A receptor 2 is also involved [24][25]. Another component that is suggested to be involved in the adhesion process of A. fumigatus is sialic acid. This component is part of a family of derivatives of neuraminic acid present on the cell surface of conidia. Removal of the surface sialic acids on the conidial surface resulted in decreased adherence of the conidia to fibronectin, suggesting that conidia adhere to basal lamina proteins via the negatively charged sugars on their surface, which are presumed to be sialic acids [26].
Other cell wall carbohydrate components also showed to mediate fungal adherence. Purified fragments of fibronectin were used to analyze which components on the conidial surface are involved in the process of adherence. The results showed that A. fumigatus conidia preferably bound to the non-glycosylated 40-kDa fragment, containing the glycosaminoglycan binding domain. Negatively charged carbohydrates, such as dextran sulfate and heparin, as well as high-ionic strength buffers, hindered binding of conidia to both fibronectin and basal lamina. This indicated that negatively charged carbohydrates on the cell wall surface of conidia may bind to the glycosaminoglycan binding domain of fibronectin and other basal-lamina proteins. Together, these data suggest that negatively charged carbohydrate moieties on the conidial surface could mediate binding to macromolecules of the host [27].
The developmentally regulating protein MedA was proposed to play an important role as an adhesin and in regulating the adherence and expression of conidiation genes. A. fumigatus mutants deficient in MedA were impaired in adherence to pulmonary epithelial cells, vascular endothelial cells and fibronectin [28]. Next to fungal adhesion to host cells, MedA also manages efficient biofilm formation, since MedA deletion mutants also showed to be decreased in biofilm formation. However, the exact molecular mechanism whereby MedA enhances adherence remains unclear.
At a later stage during biofilm formation, adhesion can also occur on a deeper level in the human host. Growing hyphae can interact with pulmonary epithelial cells, where they adhere to and invade the abluminal surface of vascular endothelial cells to eventually access the vascular compartment. When the hyphae entered the blood vessels, hyphal fragments can be distributed to other sites in the host where they can adhere to the luminal surface of endothelial cells before passing through them and invading into deep tissues. A. fumigatus hyphae can induce host cell damage and death. There, it is likely that the basal lamina within the airways and blood vessels are exposed, and that fungal cells can adhere to basement membrane macromolecules including laminin, fibronectin and collagen [17].

2.2. Conidial Germination and Hyphal Development

After attachment of A. fumigatus conidia to the surface, further colonization occurs through hyphal proliferation [14]. Additionally, as shown in a study by Wasylnka & Moore [29] with two A. fumigatus strains expressing green fluorescent protein, conidia can be internalized by nonprofessional phagocytes in vitro such as epithelial and endothelial cells to germinate at a later stage [30]. This was also observed with conidia of C. albicans, where a study showed that blastoconidia could be internalized by endothelial cells and macrophages in mice [31].
The conidial germination of A. fumigatus involves disruption of the hydrophobic rodlet layer, revealing the inner conidium walls that are composed of polysaccharides, which are hydrophilic cell wall components. During germination, a hydrophobic tip can be found on a single germinating spore. The conidium loses its surface hydrophobicity progressively and the new growth-point exhibits a coexistence of hydrophobic rodlets and hydrophilic polysaccharides [15][22].
After adhesion of the conidia, conidial germination into hyphae begins with the formation of tube-like channels that possess the hydrophobic nature of the cell wall that is suggested to enhance hyphal development [22]. In hyphal development, the adhesive exopolysaccharide galactosaminogalactan (GAG) plays an important role in adherence of A. fumigatus hyphae to cells of the human host and modulating the immune response during infection. GAG is secreted by growing hyphae, where it binds to the surfaces of these hyphae, resulting in a polysaccharide sheath covering the growing organisms [32]. The fungal regulatory protein MedA and developmental transcription factor StuA both affect the formation of adherent biofilms. Disruption of StuA in A. fumigatus strains resulted in reduced adherence to pulmonary epithelial lines and other abiotic substrates [33]. A comparative transcriptome analysis of the ΔmedA and ΔstuA regulatory mutants identified a gene encoding a putative UDP-glucose-epimerase, designated uge3, which was dysregulated in both the ΔstuA and ΔmedA mutants. Disruption of Uge3 resulted in full impairment of GAG synthesis, and markedly decreased adhesion to host cells and biofilm formation. This indicates that GAG is necessary for the efficient attachment of hyphae and biofilm structural integrity [33].
In C. albicans, a proliferation phase is also followed after attachment of the yeast cells, and initiation of filamentation will result in hyphal development, eventually leading to the biofilm development process [34]. In hyphal development, hyphal morphogenesis is important for adhesion maintenance. In this process, the proteins EFG1 and BCR1 are key regulators of several adhesin genes, including most of the ALS gene family, EAP1 and HWP1. A study by McCall et al. [35] showed that adhesion maintenance proteins in C. albicans are expressed at different times during growth phases. Whereas the adhesion maintenance protein Ywp1 is expressed during late biofilm growth, disruption of EFG1 and BCR1 in C. albicans deletion strains demonstrated poor adherence of hyphae in biofilm. This indicates that filamentation is important for further expression of adhesion maintenance proteins. Moreover, the expression of BCR1 is under the regulation of the hyphal regulator Tec1p, where BCR1 is a downstream component of the hyphal regulatory network that couples expression of cell-surface genes to hyphal differentiation. This indicates that hyphal cells are specialized to present adherence components to ensure biofilm structure and integrity [36].

2.3. Biofilm Maturation

After development of the hyphae, the process of biofilm maturation is initiated. During this stage, a biofilm matrix is formed consisting of the extracellular matrix (ECM) that covers the colony surface and binds the cells to form the structural base of the biofilm and glues the hyphae together [12][15]. In A. fumigatus, the structural components of the mature biofilm generally consist of GAG, galactomannan, α-1,3 glucans, monosaccharides, proteins, antigens and lipids, melanin, polyols, and extracellular DNA (eDNA) [13]. Additionally, an expression study showed that there are at least two hydrophobin genes (rodB and rodC) expressed in aerial static mycelium. However, no rodlet proteins were detected in the same ECM [12].
In C. albicans, the biofilm matrix is characterized by a structured mixture of pseudohyphal and hyphal cells encased by an ECM that consists of glycoproteins, carbohydrates, α-mannan and β-1,6-glucan polysaccharides, β-1,3-glucan, lipids and eDNA [16].
The structure of biofilms is dependent of the environmental conditions of the microorganism. Therefore, the biofilm structure can vary and keep reshuffling as they keep on adapting to their environment. For example, the composition of the ECM could vary between aspergillosis pathologies. In a study by Loussert et al. [37] it was shown that an ECM is produced in the lungs at the surface of A. fumigatus hyphae that are present in patients suffering from aspergilloma or IA. The ECM at these different sites showed a different hyphal organization. Light microscopic observations showed that during aspergilloma a ball of strongly agglutinated hyphae without any host cells inside was formed. Additionally, a dense material surrounded the hyphae, and at the periphery of the ball, many blood cells were identified. On the contrary, the hyphae detected in experimental IA were shown to be separated. Moreover, the ECM at these sites contained galactomannan and GAG as observed in vitro. Nevertheless, α-1,3 glucan which was also present in the ECM in vitro was detected only in aspergilloma at the periphery of the ECM. Other components, such as the major antigenic glycoproteins, were present in aspergillosis and IA ECM in vitro but were not observed in the ECM produced in vivo. A possible explanation for this effect is that these antigens are secreted during infection, but do not accumulate as much as seen in vitro, since these antigens were detected in patients with aspergillosis and IA [37].
In fungal biofilm development, the ECM that is formed contributes to the structural base of the biofilm, including the exopolymeric substance (EPS) and network of mycelia. The EPS occurs with a mucous appearance that adheres completely and covers the hyphae, forming a covering sheath over the fungal cells [15]. In the mature biofilm, the immobilized cells function as an ecosystem that includes continuous interactions in the form of cell-cell communication acting as a structured network that holds the cells together. The EPS in the ECM undertakes many important functions such as adhesion, cell aggregation, providing protection against antimicrobial agents and host defense mechanisms, providing a nutrient source, stabilization of the cell community and the exchanging of genetic information [15].
In both A. fumigatus and C. albicans, eDNA is an important component of the ECM, where it contributes to structural integrity and antifungal resistance [38][39][40]. A mechanism by which eDNA can provide biofilm resistance is by changing the extracellular environment. Since eDNA is an anionic macromolecule, this molecule is able to chelate cations such as magnesium ions, resulting in a decline of effective concentration of Mg2+ in the fungal environment. Moreover, certain concentrations of DNA can regulate the induction of the cationic antimicrobial peptide resistance operon, PA3552–PA3559 in Pseudomonas aeruginosa (P. aeruginosa). This indicates that the presence of eDNA can contribute to genomic DNA release and inducible antibiotic resistance [41].
Another role of eDNA is identified as providing the exchange of genetic information by horizontal gene transfer [42]. Several studies showed that plasmid transfer occurs at an increased rate in biofilms compared to planktonic cultures. A study by Hausner & Wuertz [43] quantified the gene transfer process in a simple laboratory-based biofilm system with a strain of Alcaligenes eutrophus as a recipient of a green fluorescent protein-tagged plasmid derivative from Escherichia coli (E. coli). The results of this experiment showed that more transconjugants occurred compared to on a plate count. The transfer of genes in eDNA can contribute to the development of antibiotic resistance in microbial populations.
In A. fumigatus, the eDNA is created by autolysis and derives from fungal cells by the secretion of chitinases by A. fumigatus, favoring its release [39]. Although it is not yet clear how eDNA contributes to antifungal resistance, treatment of A. fumigatus biofilm with DNase resulted in a destabilized integrity of the biofilm and an increased susceptibility to antifungals amphotericin B and caspofungin. Therefore, it is suggested that the presence of eDNA reduces exposure of the target cells to the antifungal drugs [13].
In C. albicans as well as A. fumigatus, a large part of the ECM consists of components of the host when grown in vivo. A previous study showed that in three infection site models of C. albicans, a biofilm matrix was produced containing host components such as hemoglobin, albumin, and alpha globulins, amylase, fibrinogen and keratin. The presence of host components also depended on the biofilm surface (venous catheter, urinary catheter or denture model). Although the precise role of these host components in the biofilms are not yet clear, the attraction of blood cells could be beneficial in the acquisition of iron. Moreover, another explanation could be that the host components are used for the structure of the biofilm to save energy by producing these components themselves [44][45].

2.4. Cell Dispersion

The stage of cell dispersion is generally considered as the terminal stage of biofilm development, also referred to as seeding dispersal [46]. Cell dispersion typically occurs in response to stressful environmental changes, where dissemination allows viable cells to persist in other locations of the host where it can further reproduce [15]. In cell dispersion of A. fumigatus, the part comprising the conidia or hyphae are detached from the biofilm. In the study of González-Ramírez et al. [15], asynchronous biofilm development was observed, in particular at the biofilm-maturation stage when the new conidia were capable of germinating, producing new mycelial growth and hyphal modifications prior to dispersion. In C. albicans, the cells dispersed from a biofilm are yeast cells that originate from the topmost hyphal layers of the biofilm [47]. In C. albicans, the dispersion of round, yeast-form cells are suggested to occur during biofilm development, but larger amounts of yeast cells are dispersed when the biofilm is in a more mature stage. Cell dispersion can lead to novel biofilm formation in the host, possibly leading to systemic infections in the bloodstream or to the spreading of the infection to other parts of the host. Known transcriptional regulators that are involved in C. albicans cell dispersion are Ume6, Nrg1 and Pes1 (also known as Nop7). Also, a component of a chromatin-modifying complex, known as Set3, is required for dispersal. Set3 is suggested to be recruited by the transcriptional regulator Nrg1 [16]. The heat shock protein 90 (Hsp90) is suggested to play a role in cell dispersion of C. albicans. Experiments performed in vitro showed that inactivation of Hsp90 reduced C. albicans biofilm growth and maturation and reduced dispersal of biofilm cells [48].

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Subjects: Agriculture, Dairy & Animal Science
Contributor MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register : Hans de Cock
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Update Date: 26 Jan 2022
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