Aspergillus galactosaminogalactan mediates adherence to host constituents and conceals hyphal β-glucan from the immune system
Open accessAbstract
Aspergillus fumigatus is the most common cause of invasive mold disease in humans. The mechanisms underlying the adherence of this mold to host cells and macromolecules have remained elusive. Using mutants with different adhesive properties and comparative transcriptomics, we discovered that the gene uge3, encoding a fungal epimerase, is required for adherence through mediating the synthesis of galactosaminogalactan. Galactosaminogalactan functions as the dominant adhesin of A. fumigatus and mediates adherence to plastic, fibronectin, and epithelial cells. In addition, galactosaminogalactan suppresses host inflammatory responses in vitro and in vivo, in part through masking cell wall β-glucans from recognition by dectin-1. Finally, galactosaminogalactan is essential for full virulence in two murine models of invasive aspergillosis. Collectively these data establish a role for galactosaminogalactan as a pivotal bifunctional virulence factor in the pathogenesis of invasive aspergillosis.
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GAG can directly enhance adhesion of A. fumigatus to host cells or material surfaces.
“It has been proven that GAG can directly enhance adhesion of A. fumigatus to host cells or material surfaces [80].”
From Antifungal persistence: Clinical relevance and mechanisms (2025) · cites this paper as [80]
A. fumigatus adherence to the epithelium is mediated by sialic acid, galactosaminogalactan, and β−1,3-glucan binding to Dectin-1.
“A. fumigatus adherence to the epithelium is mediated by several fungal factors, including sialic acid (SA), galactosaminogalactan (GAG) and β−1,3-glucan binding to Dectin-1 [171–173].”
From Mechanisms of fungal dissemination (2021) · cites this paper as [172]
Several enzymes associated with a putative GAG synthesis cluster in chromosome 3 have been identified recently.
“Several enzymes associated with a putative GAG synthesis cluster in chromosome 3 have been identified recently (480, 482, 483).”
From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [482]
GAG masks PAMP exposure and the subsequent release of CXC chemokines regulating neutrophil recruitment.
“It masks PAMP exposure and the subsequent release of CXC chemokines regulating neutrophil recruitment (482).”
From Aspergillus fumigatus and Aspergillosis in 2019 (2019) · cites this paper as [482]
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References 51 · Cited by 320
Research works printed but not linked: 1
- [2]Denning DW (2000) Aspergillus species. In: Mandell GL, Bennett JE, Dolin R, editors. Mandell, Douglas, and Bennett's principals and practice of infectious diseases. 5th ed. Philadelphia: Chuchill Livingston. pp. 2674–2685.
- Authors
- Gravelat, F. N., Beauvais, A., Liu, H., Lee, M. J., Snarr, B. D., Chen, D., Xu, W., Kravtsov, I., Hoareau, C. M. Q., Vanier, G., Urb, M., Campoli, P., Al Abdallah, Q., Lehoux, M., Chabot, J. C., Ouimet, M.-C., Baptista, S. D., Fritz, J. H., Nierman, W. C., Latgé, J. P., Mitchell, A. P., Filler, S. G., Fontaine, T., & Sheppard, D. C.
- Affiliations
- McGill University (CA)
- Institut Pasteur (FR)
- University of California, Los Angeles (US)
- J. Craig Venter Institute (US)
- Carnegie Mellon University (US)
- Corresponding author
- Fontaine, Thierry
- Sheppard, Donald C.
- ORCID
- Venue
- PLoS Pathogens
- Publisher
- Public Library of Science (PLoS)
- Published
- 2013-08-22
- Volume
- 9
- Issue
- 8
- Pages
- e1003575
- ISSN
- 1553-7366 (ISSN-L)
- 1553-7374
- PMC
- PMC3749958
- OpenAlex
- W2048550577
- Cited by
- 320
- References
- 51
- Citations by year
- 2026: 19 · 2025: 24 · 2024: 20 · 2023: 26 · 2022: 26 · 2021: 43 · 2020: 35 · 2019: 22 · 2018: 21 · 2017: 18 · 2016: 30 · 2015: 17 · 2014: 16 · 2013: 3
- FWCI
- 15.88
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS Pathogens (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, cc-by)
- eScholarship@McGill (McGill) (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship@McGill (McGill) (submittedVersion, cc-by)
- eScholarship (California Digital Library) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- Cystic Fibrosis Canada
- European Commission (260338)
- Agence Nationale de la Recherche (ANR-06-EMPB-0011)
- National Institutes of Health (UL1TR000124, n01ai30041-9-0-1, 30041)
- Canadian Institutes of Health Research
- National Institute of Allergy and Infectious Diseases (N01 AI30041, N01 AI030041, R01AI073829)
- National Center for Advancing Translational Sciences
- Topics
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
- Keywords
- Aspergillus fumigatus, invasive aspergillosis, galactosaminogalactan, fungal adhesion, epimerase, adhesins, Dectin-1, host immune evasion, fibronectin, epithelial cells, fungal virulence, inflammatory response suppression
- MeSH terms
- Dectin-1, Animals, Aspergillosis, Aspergillus fumigatus, Carbohydrate Epimerases, Cell Line, Disease Models, Animal, Fungal Proteins, Humans, Polysaccharides, Hyphae, Lectins, C-Type, Virulence Factors, beta-Glucans, Mice, Fungal Polysaccharides
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