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Oliver C. Grant

Researcher at University of Georgia

Publications -  45
Citations -  2120

Oliver C. Grant is an academic researcher from University of Georgia. The author has contributed to research in topics: Glycan & Glycosylation. The author has an hindex of 21, co-authored 45 publications receiving 1426 citations. Previous affiliations of Oliver C. Grant include National University of Ireland & National University of Ireland, Galway.

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Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor.

TL;DR: Glycomics-informed glycoproteomics is utilized to characterize site-specific microheterogeneity of glycosylation for a recombinant trimer Spike mimetic immunogen and for a soluble version of human ACE2, which can facilitate immunogen design to achieve antibody neutralization and inform therapeutic strategies to inhibit viral infection.
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Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition.

TL;DR: 3D structures show that the protein surface is extensively shielded from antibody recognition by glycans, with the notable exception of the ACE2 receptor binding domain, and also that the degree of shielding is largely insensitive to the specific glycoform.
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Characterization of heparin and severe acute respiratory syndrome-related coronavirus 2 (SARS-CoV-2) spike glycoprotein binding interactions.

TL;DR: Use of a surface plasmon resonance direct binding assay and unbiased computational ligand docking indicates that heparan sulfate interacts with the GAG-binding motif at the S1/S2 site on each monomer interface in the trimeric SARS-CoV-2 SGP, and at another site when the receptor-binding domain is in an open conformation.
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Recent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity

TL;DR: Using an influenza receptor glycan microarray with extended airway glycans, it is found that H3N2 viruses have in fact maintained human-type specificity, but they have evolved preference for a subset of receptors comprising branched glycans with extended poly-N-acetyl-lactosamine (poly-LacNAc) chains.
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Integrated Omics and Computational Glycobiology Reveal Structural Basis for Influenza A Virus Glycan Microheterogeneity and Host Interactions

TL;DR: A study that integrates proteomics, glycomics and glycoproteomics of HA before and after adaptation to innate immune system pressure to better define the relationships among glycosylation, viral bioactivity and evolution.