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Functional Amyloids in Adhesion of Non-albicans Candida Species

Summary

Candida fungi cause common infections and form tough biofilms that resist treatment. These fungi stick to body surfaces using proteins called adhesins that form amyloid-like structures. Researchers found that special peptides can block these amyloid structures in several Candida species, preventing them from sticking to cells and potentially offering a new way to fight these infections.

Background

Candida fungal species are the most common fungal opportunistic pathogens, with increasing prevalence of non-albicans species like C. tropicalis and C. parapsilosis. These fungi express surface-anchored adhesins containing cross-β core sequences that form amyloid-like protein aggregates, contributing to biofilm formation and antifungal resistance.

Objective

To determine whether Als-amyloid-binding and Als-anti-amyloid peptides can identify and inhibit amyloid-like interactions on the cell surface of non-albicans Candida species (C. tropicalis, C. krusei, and C. parapsilosis) and test their effects on fungal cell aggregation and epithelial cell adhesion.

Results

The Als-amyloid-binding peptide bound to C. albicans, C. tropicalis, and C. parapsilosis, with dim staining in C. krusei. C. tropicalis aggregates were thioflavin T positive and aggregation was blocked by the Als-anti-amyloid peptide. The anti-amyloid peptide inhibited adhesion of C. albicans, C. tropicalis, and C. parapsilosis to epithelial cell monolayers by >80%, but had no effect on C. krusei.

Conclusion

Amyloid-like interactions mediated by Als family adhesins function in pathogenesis across multiple Candida species. The conservation of cross-β core sequences in Als adhesins of C. tropicalis and C. parapsilosis supports the involvement of functional amyloids in biofilm formation and host adhesion in these clinically important non-albicans species.
  • Published in:Pathogens,
  • Study Type:Experimental Research,
  • Source: PMID: 40872233, DOI: 10.3390/pathogens14080723
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