An NSF-funded biofoundry at the Complex Carbohydrate Research Center, providing the analytical services, reagents, computational tools and training that make glycoscience accessible to every laboratory.
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Research, education and training in glycoscience
Glycans decorate the surface of every cell and most secreted proteins, where they govern recognition, adhesion, signalling and stability. They remain difficult to work with: the reagents are hard to obtain, the analytical methods are specialised, and the instrumentation sits in a small number of centres. BioF:GREAT exists to lower each of those barriers — and to bring glycoscience into the classroom.
Glycomics, glycoproteomics, monosaccharide composition, linkage analysis, glycolipids, sialic acids and glycosylation site mapping by HPAEC, GC-MS, MALDI-TOF/TOF, Orbitrap MS and NMR.
Recombinant GFP-tagged glycosyltransferases in 100 µg units, with nucleotide-sugar donors and analogs for chemoenzymatic synthesis.
Nucleotide-sugar donors, azido sugar analogs and protected derivatives synthesised in house at >95% purity, for chemoenzymatic synthesis and bioorthogonal labelling.
Antibodies and antibody-based reagents for glycan detection, in development and available soon — register interest in a target epitope and application.
Deep learning for glycoenzyme classification and function prediction, GTXplorer, and JAAG for AlphaFold 3 glycan modelling.
23 internal and 29 external projects spanning structural glycobiology, glycoproteomics, glycan engineering and computational method development.
Summer bench courses and virtual courses in carbohydrate and glycoconjugate analysis, for students, postdoctoral researchers and visiting scientists.
Instructional modules, case studies, videos and scientist interviews — developed, evaluated and revised on the basis of education research.
BioF:GREAT is bringing Daniel A. Polasky of the Nesvizhskii laboratory at the University of Michigan to the CCRC for a hands-on workshop on MSFragger and FragPipe, alongside a seminar on 20 August 2026.
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The Complex Carbohydrate Research Center will host a one-day glycoscience symposium, Glycans in Health and Disease, on 24 June 2026.
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BioF:GREAT investigators, postdoctoral researchers and students hosted and attended sessions at ACS Spring 2026 in Atlanta, presenting across glycoanalytics, glycoenzyme engineering and glycoscience education.
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Lance Wells, principal investigator of BioF:GREAT, has been named a Fellow of the American Society for Biochemistry and Molecular Biology.
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Episode 61 of Let’s Talk Chemistry covers XLID, O-GlcNAc and how glycosylation can be used to make drugs more effective.
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More in highlights and news and events and conferences.
Peer-reviewed work from the BioF:GREAT laboratories and their collaborators. Summaries state each paper’s own reported finding; figures are from the papers themselves.
Crystal structure of a β1,3-Glucosyltransferase reveals an unusual substrate recognition by a two-domain GT-A fold glycosyltransferase.
B3GLCT extends the rare O-fucose modification on thrombospondin type 1 repeats, and pathogenic variants cause Peters Plus syndrome. Unusually for its fold family, it carries a second GT-A domain — and the crystal structure of the enzyme bound to an O-fucosylated repeat shows that domain is essential for substrate binding yet catalytically dead: it binds neither UDP nor Mn2+, and its vestigial active site faces away from where the substrate sits.
Building Bridges: A Story of How Institutional Investment in Discipline-Based Education Research Enables Evidence-Based Teaching in Biochemistry Education.
Discoveries reach the literature faster than they reach undergraduate teaching, which is why glycoscience is largely absent from the curriculum. This account describes how institutional investment in discipline-based education research faculty at UGA lets disciplinary scientists and education researchers co-develop teaching materials that are both current and built around how students actually learn — with BioF:GREAT’s education arm as the worked example.
Structural basis of chondroitin sulfate backbone polymer synthesis.
Four homologous proteins build the chondroitin sulfate backbone, and this work shows why they need each other: one CHPF and one CHSY must be co-expressed to form a soluble, functional heterodimer. Cryo-EM of CHSY3-CHPF1 plus mutagenesis places both catalytic activities in the CHSY subunit — its GT31 domain transfers β1,3-GlcA and its GT7 domain β1,4-GalNAc — while the CHPF domains contribute no synthesis and instead stabilise their CHSY counterparts.
Inhibition of endocytosis by glycans arises from steric rather than electrostatic repulsion.
Glycosylation slows the uptake of membrane proteins by clathrin-mediated endocytosis, but it was unclear whether the barrier is steric bulk or negative charge. Stripping sialic acid from a densely O-glycosylated ligand changed neither receptor uptake nor the ligand’s hydrodynamic radius, pointing to steric bulk rather than electrostatic repulsion.
Chemoenzymatic Synthesis of N-Linked Glycan Receptors of H1N1 Influenza Virus on Human Airway Epithelial Cells.
Glycomics of human nasal and tracheal epithelium guided the chemoenzymatic synthesis of a library of α2-6 sialylated N-glycans representing the receptors influenza actually meets in the airway. Screening hemagglutinins from the 1918 and 2009 H1N1 pandemics showed that receptor specificity has changed remarkably little across a century: both prefer biantennary glycans carrying two or more LacNAc repeats on at least one antenna.
Rapid elicitation of neutralizing Asn332-glycan-independent antibodies to the V3-glycan epitope of HIV-1 Env in nonhuman primates.
Eliciting broadly neutralizing antibodies against HIV-1 normally takes repeated immunizations over long periods. WIN332, an engineered envelope immunogen, raised antibodies against the conserved V3-glycan epitope after a single dose in nonhuman primates — including a first-of-its-class type that does not depend on the Asn332 glycan.
The full list is on the publications page.
BioF:GREAT works through collaborations — between laboratories at the Complex Carbohydrate Research Center, and with partners at other universities, national laboratories, agencies and companies. A sample of current work:
Internal · Labs: Moremen and Perez
Cryo-EM and enzymology on the machinery that polymerises the chondroitin sulfate backbone, published in Nature Communications this year.
Internal · Labs: Moremen, Weiss, Perez and Ramirez
Reconstituting the glycosaminoglycan biosynthetic pathway as assembled complexes rather than isolated enzymes, to ask how chain length and sulfation are controlled.
Internal · Labs: Kannan
Machine-learning models that predict which sugar donor an uncharacterised glycoenzyme uses, narrowing the experiments needed to assign function across large enzyme families.
External · Labs: Wells and Kong
Adding engineered glycans to virus-like particles so the immune response focuses on the conserved HIV-1 fusion peptide instead of the carrier.
External · Labs: Moremen, Urbanowicz and Scheller
Engineering the enzymes that build plant cell wall polysaccharides, with applications from biofuel feedstocks to plant-derived materials.
External · Labs: Dolan, multi-university student collaboration
Undergraduate teaching modules built and tested across several institutions, addressing how little glycoscience reaches the classroom before graduate level.
The full portfolio is listed under internal projects and external projects.