Related Experiment Video
Updated: Sep 9, 2025
Determination of Biofilm Initiation on Virus-infected Cells by Bacteria and Fungi
Published on: July 6, 2016
Functional Amyloids in Adhesion of Non-albicans Candida Species
Melissa C Garcia-Sherman1, Safraz A Hamid1, Desmond N Jackson1
1Department of Biology, Brooklyn College of the City University of New York, Brooklyn, NY 11215, USA.
Abstract:
Candida fungal species are the most common fungal opportunistic pathogens. Their ability to form antifungal resistant biofilms contributes to their increasing clinical frequency. These fungi express surface-anchored adhesins including members of the Als family. These adhesins mediate epithelial adhesion, aggregation, and biofilm formation. Many of the adhesins contain cross-β core sequences that form amyloid-like protein aggregates on the fungal surface. The aggregates mediate high-avidity bonding that contributes to biofilm establishment and persistence. Accordingly, autopsy sections from individuals with candidiasis and other mycoses have amyloids within abscesses. An amyloid-forming peptide containing a sequence from Candida albicans Als5 bound to C. albicans, C. tropicalis, and C. parapsilosis. C. albicans and C. tropicalis aggregated with beads coated with serum albumin, and the aggregates stained with the amyloid-binding dye thioflavin T. Additionally, an Als5-derived amyloid-inhibiting peptide blocked cell aggregation. The amyloid-inhibiting peptide also blocked C. albicans, C. tropicalis, and C. parapsilosis adhesion to monolayers of FaDu epithelial cells. These results show the involvement of amyloid-like interactions in pathogenesis in several Candida species.
Insights
Candida fungi form biofilms using amyloid-like protein aggregates on their surface. Inhibiting these amyloid interactions reduced fungal aggregation and adhesion, offering new therapeutic targets for candidiasis.
Area of Science:
- Mycology
- Infectious Diseases
- Biochemistry
Background:
- * *Candida* species are common opportunistic fungal pathogens, frequently causing infections.
- * Antifungal-resistant biofilms formed by *Candida* contribute to their rising clinical prevalence.
- * Surface-anchored adhesins, like the Als family, mediate fungal adhesion, aggregation, and biofilm formation.
Purpose of the Study:
- * To investigate the role of amyloid-like protein aggregates in *Candida* pathogenesis.
- * To determine if amyloid interactions contribute to biofilm formation and host cell adhesion in multiple *Candida* species.
Main Methods:
- * An amyloid-forming peptide from *Candida albicans* Als5 was used to study binding.
- * Aggregation assays were performed using serum albumin-coated beads and stained with thioflavin T.
- * An Als5-derived amyloid-inhibiting peptide was tested for its effect on fungal aggregation and epithelial cell adhesion.
Main Results:
- * An amyloid-forming peptide bound to *Candida albicans*, *C. tropicalis*, and *C. parapsilosis*.
- * *C. albicans* and *C. tropicalis* formed aggregates with albumin-coated beads, which stained positive for amyloid.
- * An amyloid-inhibiting peptide successfully blocked fungal aggregation and adhesion to epithelial cells.
Conclusions:
- * Amyloid-like interactions are involved in the pathogenesis of several *Candida* species.
- * Targeting these amyloid interactions presents a potential strategy for treating candidiasis.
Related Concept Videos
03:03Amyloid Fibrils
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
01:23Surface Appendages of Archaea