Structure and Function of UDP-GalNAc:polypeptide alpha-GalNAc transferases

NIH Pandemic-Era Grants

Pandemic Era Grants

2020

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Principal Investigator: Lawrence A. Tabak
Organization: NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH
Fiscal Year: 2020
Award: $911,573
Funding agency: National Institute of Dental and Craniofacial Research

Our lab studies the structure and function of GalNAc-Ts. in collaboration with Kelly Ten Hagen, NIH and Tom Gerkin, CWRU, we published a paper describing how the differential splicing of the lectin domain of a GalNAc-T modulates both peptide and glycopeptide preferences. We have also submitted a methods paper to Glycoconjugate J. on mapping O-glycans using solid phase extraction (SPE) enrichment, protease digestion, and Electron-transfer/Higher Energy Collision Dissociation (EThcD) fragmentation. This work utilized O- protease to specifically cleave O-glycosites and studied the influence of negatively charged amino acids and sialic acids on O-glycosite localization. 

During the pandemic we have performed in silico modeling of potential O-glycan sites on the spike protein of Sars-Cov-2. We are now back in the lab on a limited basis and are mapping O-glycans from recombinantly expressed spike protein in E. coli (negative control), HEC cells, and Bacculovirus.

Terms: <2019 novel coronavirus><2019-nCoV><Acetylgalactosamine><Amino Acids><Back><Biological Function><Biological Process><Cell Body><Cells><Charge><Cleaved cell><Collaborations><Core Protein><Digestion><Dissociation><Dorsum><E coli><E. coli><EC 2.4><Electron Transport><Escherichia coli><Esteroproteases><Event><GalNAc-T8><GalNAc-transferase><GalNAcT-8><Glycoconjugates><Glycopeptides><Glycoproteins><Glycoside Transferases><Glycosides><Goals><Golgi><Golgi Apparatus><Golgi Complex><L-Serine><L-Threonine><Laboratories><Lectin><Link><Methods><Modeling><Molecular><Mucins><Mucus Glycoprotein><N acetylgalactosamine><N-Acetylneuraminic Acids><NIH><National Institutes of Health><Oligosaccharides><Paper><Peptidases><Peptide Hydrolases><Peptides><Phase><Polypeptide N-acetylgalactosaminyltransferase><Protease Gene><Proteases><Proteinases><Proteins><Proteolytic Enzymes><Publishing><RNA Splicing><Recombinants><SARS-CoV-2><SARS-CoV2><SARS-associated coronavirus 2><SARS-coronavirus-2><SARS-related coronavirus 2><Serine><Severe acute respiratory syndrome coronavirus 2><Sialic Acids><Site><Solid><Splicing><Structure><Threonine><Tn antigen><UDP-GPAGAT><UDP-GalNAc-polypeptide N-acetylgalactosaminyltransferase><UDP-N-acetylgalactosamine mucin transferase><UDP-N-acetylgalactosamine-polypeptide N-acetylgalactosamine transferase><UDPacetylgalactosamine-protein acetylgalactosaminyltransferase><United States National Institutes of Health><Work><Wuhan coronavirus><aminoacid><cleaved><electron transfer><glycosyltransferase><in silico><pandemic><pandemic disease><polypeptide><preference><protein-UDPacetylgalactosaminyltransferase><sugar>