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Engineering a therapeutic lectin by uncoupling mitogenicity from antiviral activity
Michael D Swanson1, Daniel M Boudreaux2, Loïc Salmon3
1Division of Infectious Diseases, Department of Internal Medicine, Program in Immunology, University of Michigan, Ann Arbor, MI 48109, USA; Division of Infectious Diseases, Department of Medicine and UNC AIDS Center, University of North Carolina, Chapel Hill, NC 27599, USA.
Altering a single amino acid in banana lectin reduces its cell-stimulating (mitogenic) activity while maintaining its broad antiviral effects. This fine-tuning offers new therapeutic tools and insights into the Sugar Code.
Area of Science:
- Carbohydrate Chemistry
- Structural Biology
- Molecular Biology
Background:
- Lectins are key players in the Sugar Code, regulating cellular functions by binding to glycans.
- Understanding lectin interactions is crucial for developing targeted therapies.
Purpose of the Study:
- To investigate the impact of a specific amino acid substitution (Histidine 84 to Threonine) in banana lectin.
- To determine how this alteration affects lectin's mitogenicity and antiviral activity.
Main Methods:
- X-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy to analyze protein structure.
- Glycocluster assays to assess carbohydrate binding interactions.
- Comparative analysis of wild-type and mutant banana lectin.
Main Results:
- A single amino acid substitution (H84T) significantly reduced banana lectin's mitogenicity.
- Antiviral potency was preserved, indicating selective modulation of lectin functions.
- Loss of mitogenicity correlated with disrupted pi-pi stacking and reduced multivalent binding.
Conclusions:
- Fine-tuning lectin structure can selectively modulate biological activities.
- This approach provides a method to separate mitogenic and antiviral functions of lectins.
- Findings offer potential for developing novel therapeutics and advancing the understanding of the Sugar Code.
