Tools for investigating host-microbe crosstalk using glycan analysis probes inspired by human lectins

Area of Science:

• Immunology
• Glycobiology
• Biochemistry

Background:

• Human lectins are key carbohydrate-binding proteins involved in host-microbe interactions.
• The specific glycan ligands and functions of many human lectins are not well understood.
• Understanding these interactions is crucial for host defense and disease research.

Purpose of the Study:

• To develop and characterize novel glycan analysis probes (GAPs) from human soluble lectins.
• To provide robust tools for investigating glycan-mediated interactions in various biological contexts.
• To enable deeper understanding of host-microbe communication and lectin function.

Main Methods:

• Protein engineering platform for scalable production of GAPs with native-like conformations.
• Incorporation of functional reporter tags for targeted glycan profiling.
• Application of GAPs in glycan arrays, mucin-binding assays, tissue staining, and microbe binding studies.

Main Results:

• Ten new GAPs were generated from diverse human soluble lectins.
• GAPs successfully maintained native-like conformations and oligomerization states.
• GAPs demonstrated utility in diverse applications, including profiling glycan interactions with microbes and host tissues.

Conclusions:

• The developed GAPs are versatile tools for dissecting glycan-mediated interactions.
• These probes facilitate the study of host responses to microbes and differential glycan recognition.
• GAPs hold potential for diagnostics in chronic diseases, dysbiosis, and immune conditions.