Human Antimicrobial Peptide LL-37 Inhibits Adhesion of Candida albicans by Interacting with Yeast Cell-Wall Carbohydrates
Open accessAbstract
Candida albicans is the major fungal pathogen of humans. Fungal adhesion to host cells is the first step of mucosal infiltration. Antimicrobial peptides play important roles in the initial mucosal defense against C. albicans infection. LL-37 is the only member of the human cathelicidin family of antimicrobial peptides and is commonly expressed in various tissues and cells, including epithelial cells of both the oral cavity and urogenital tract. We found that, at sufficiently low concentrations that do not kill the fungus, LL-37 was still able to reduce C. albicans infectivity by inhibiting C. albicans adhesion to plastic surfaces, oral epidermoid OECM-1 cells, and urinary bladders of female BALB/c mice. Moreover, LL-37-treated C. albicans floating cells that did not adhere to the underlying substratum aggregated as a consequence of LL-37 bound to the cell surfaces. According to the results of a competition assay, the inhibitory effects of LL-37 on cell adhesion and aggregation were mediated by its preferential binding to mannan, the main component of the C. albicans cell wall, and partially by its ability to bind chitin or glucan, which underlie the mannan layer. Therefore, targeting of cell-wall carbohydrates by LL-37 provides a new strategy to prevent C. albicans infection, and LL-37 is a useful, new tool to screen for other C. albicans components involved in adhesion.
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Glucans are major cell wall components in fungi and exoglucanases are involved in cell wall modification, cell adhesion, and killer toxin resistance.
“Glucans are major cell wall components in fungi and exoglucanases are involved in cell wall modification, cell adhesion, and killer toxin resistance (Adams 2004; Jiang et al. 1995; Tsai et al. 2011; Xu et al. 2013).”
From Biocontrol yeasts: mechanisms and applications (2019) · cites this paper as Tsai et al. 2011
The Discussion describes glucan as a layer of the C. albicans cell wall, supporting its role as a cell-wall component. It does not establish that exoglucanases modify the wall, mediate adhesion, or confer killer-toxin resistance; its adhesion findings concern LL-37 and cell-wall carbohydrates. Page numbers are not available in our copy. (LLM, conf=0.87)
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- Authors
- Tsai, P.-W., Yang, C.-Y., Chang, H.-T., & Lan, C.-Y.
- Affiliations
- National Tsing Hua University (TW)
- Animal Technology Institute Taiwan (TW)
- China Medical University (TW)
- Corresponding author
- Chang, Hao-Teng
- Lan, Chung-Yu
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2011-03-14
- Volume
- 6
- Issue
- 3
- Pages
- e17755
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC3056723
- OpenAlex
- W2167693400
- Cited by
- 175
- References
- 75
- Citations by year
- 2026: 15 · 2025: 9 · 2024: 10 · 2023: 10 · 2022: 13 · 2021: 16 · 2020: 13 · 2019: 10 · 2018: 11 · 2017: 7 · 2016: 12 · 2015: 12 · 2014: 11 · 2013: 12 · 2012: 10
- FWCI
- 10.94
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- PLoS ONE (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- National Science Council
- China Medical University
- Topics
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
- Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
- Keywords
- LL-37, cathelicidin, antimicrobial peptides, Candida albicans, fungal adhesion, mannan, cell wall carbohydrates, chitin, glucan, yeast aggregation, oral epithelial cells, urinary bladder, mucosal protection, fungal infection prevention
- MeSH terms
- Epidermal Cells, Adhesiveness, Animals, Urinary Bladder, Candida albicans, Cell Wall, Epidermis, Humans, Polystyrenes, Protein Binding, Antimicrobial Cationic Peptides, Carbohydrate Metabolism, Microbial Viability, Mice, Cathelicidins
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