earticle

영어

Cell surface glycans lie at the interface between the cell and its environment, playing an active role in mediating interactions with foreign substances. Although current lectin-based methods enable detection of select glycan epitopes present on the cell surface, detailed structural information of glycan heterogeneity is needed to better assess their involvement in cell-cell interactions, particularly with pathogens. Mass spectrometry-based glycomics has the potential to provide a single platform to monitor hundreds of native structures simultaneously. This study constitutes a comprehensive and quantitative analysis that defines the sequence of oligosaccharides on human cells that affect the nature of Salmonella Typhimurium infection. We first examined the glycan products remaining on the host cell surface after brief contact with bacteria, which included mainly, desialylated and high mannose glycans. We then describe a glycomic landscaping (glycoscaping) strategy to present predominantly high mannose glycans on host cells to better correlate phenotype with structure. A better understanding of the biological roles of glycosylation is achieved by structure-specific re-engineering towards specified glycosylation patterns. Changes in the glycan landscape were induced on live cells, using a mixture of glycosidases and glycosidase inhibitors. Following treatment, the exact changes were characterized by mass spectrometry. Such glycoscaping, when applied to intestinal epithelial cells, yielded significant increases in membrane enzyme activity, cell permeability, migration, and microbial infection.