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Our lab studies the glycobiology of protozoan parasites that cause diarrhea (Cryptosporidium and Giardia), dysentery (Entamoeba), birth defects (Toxoplasma), and blindness (Acanthamoeba). In particular, we use mass spectrometric, biochemical, and genetic methods to characterize sugars added to glycoproteins, as well as the enzymes that make or remove these sugars (glycosyltransferases and glycosyl hydrolases, respectively). For example, we showed that asparagine-linked glycans (N-glycans) of Cryptosporidium have a single mannose arm that is hardly modified and so is distinct from complex, highly modified N-glycans of the host. In contrast, Cryptosporidium vaccine candidates have mucin-like domains densely modified with O-GalNAc that resemble host intestinal mucins. We discovered a large set of nuclear proteins of Toxoplasma that are decorated with O-linked fucose and showed that O-fucosyltransferase is a homolog of plant Spindly. The host is lacking Spindly but has an O-GlcNAc transferase with a similar structure to Spindly that modifies an even larger set of nucleocytosolic proteins. We also identified a second Toxoplasma O-fucosyltransferase that modifies a secreted protein MIC2, which is essential for parasite adherence to and invasion into host cells.
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biorxiv(2024)
Christopher M. West, Megna Tiwari, Hanke Welvan der,Ana Maria Garcia,Macy M. Willis,Hyunwoo Kim,Giulia Bandini,Maissa M. Gaye,Catherine E. Costello,John Samuelson
GLYCOBIOLOGYno. 11 (2022)
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