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Biochemical and Structural Studies of Target Lectin SapL1 from the Emerging Opportunistic Microfungus Scedosporium apiospermum

Summary

This research identified and characterized a new protein (SapL1) from an emerging fungal pathogen that causes serious infections in humans, especially in people with weakened immune systems. The protein helps the fungus attach to human cells by recognizing specific sugar molecules on their surface. Understanding how this protein works could lead to new treatments for fungal infections. Impacts on everyday life: • Could lead to new treatments for fungal infections that are safer than current antifungal drugs • Particularly important for cystic fibrosis patients who are vulnerable to these infections • Advances our understanding of how harmful fungi cause infections • May help develop preventive treatments for high-risk patients • Could inspire new approaches to fighting other fungal diseases

Background

Scedosporium apiospermum is an emerging opportunistic fungal pathogen that causes life-threatening infections in humans, particularly in immunosuppressed patients. Host-pathogen interactions often involve lectins, which have become therapeutic targets for developing carbohydrate mimics for antiadhesive therapy. Understanding these interactions is crucial for developing new treatments against fungal infections.

Objective

To identify, characterize, and analyze the first lectin (SapL1) from S. apiospermum, investigating its role in host-pathogen interactions and potential as a therapeutic target. The study aimed to determine the protein’s structure, binding properties, and interaction with human bronchial epithelial cells.

Results

SapL1 showed specificity for fucosylated oligosaccharides with submicromolar affinity for fucose. The crystal structure revealed a six-bladed β-propeller fold with six binding sites. The protein demonstrated binding to bronchial epithelial cells in a fucose-dependent manner. The presence of osmolytes was crucial for achieving soluble protein expression in bacteria.

Conclusion

SapL1 is the first characterized lectin from S. apiospermum that recognizes and binds to fucosylated human glycoconjugates. The detailed structural and functional information gathered positions SapL1 as a promising target for developing antiadhesive glycodrugs against Scedosporium infections. The study provides crucial insights into the host-binding process during early infection stages.
  • Published in:Scientific Reports,
  • Study Type:Biochemical and Structural Analysis,
  • Source: 10.1038/s41598-021-95008-4
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