Catanionic Surfactant Vesicles as a New Platform for Probing Glycan–Protein Interactions

Glycomics lags substantially behind proteomics and genomics in its ability to decipher and synthesize complex glycans. The slow progress in deciphering glycan interactions at a molecular level is in large part due to the absence of a functional system to express, on a large scale, carbohydrates of known structure, in the context of a biologically relevant assay system. Here, the characterization of glycan‐functionalized catanionic surfactant vesicles (CVs) as a platform for glycan synthesis is described, and it is demonstrated that the resulting glycan‐functionalized CVs can serve as a scaffold for the interrogation of protein‐glycan interactions. It is demonstrated that Neisseria gonorrhoeae lipooligosaccharide (LOS) glycosyltransferase LgtE, an enzyme that catalyzes the addition of galactose onto a terminal glucose found on LOS, can be used to biochemically modify LOS or glucose functionalized CVs. CVs are characterized by differential lectin binding using flow cytometry. LgtE activity is measured on whole cells and LOS functionalized vesicles and found to have approximately the same biochemical properties. It is further demonstrated that CVs can be inkjet printed. This paper presents proof‐of‐concept that glycan‐functionalized catanionic vesicles can be used to create a high‐specificity and high‐throughput glycan array that will allow for the investigation of a variety of protein–glycan interactions.