The Glycobiology Core will provide a resource for all Center members providing expertise and facilities in glycan/glycoprotein engineering and structural analysis of glycans. Approximately half of the molecular mass of HIV gp120 is comprised of N-linked glycans that shield the protein backbone. These glycans impact on vaccine design in three distinct ways. Firstly, the carbohydrates themselves are distinct from typical human glycosylation and can serve as a target for broadly neutralizing antibodies. Secondly, the glycans of gp120 limit or modulate antibody recognition of underlying protein epitopes. Finally, both viral (and immunogen) glycans can interact with host cell lectins and trigger major immunomodulatory signaling pathways. The Glycobiology Core is devoted to supporting Center members in the optimization of these critical parameters for vaccine design.
The Glycobiology Core will contribute to the development of immunogens by the provision of a range of analytical tools (NP-HPLC, MALDI-MS, ESI-MS/MS and Ion Mobility MS) and provide full compositional and linkage information on viral and immunogen glycans.
|Sok, Devin; Doores, Katie J; Briney, Bryan et al. (2014) Promiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV. Sci Transl Med 6:236ra63|
|Murin, Charles D; Julien, Jean-Philippe; Sok, Devin et al. (2014) Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy. J Virol 88:10177-88|
|Scharf, Louise; Scheid, Johannes F; Lee, Jeong Hyun et al. (2014) Antibody 8ANC195 reveals a site of broad vulnerability on the HIV-1 envelope spike. Cell Rep 7:785-95|
|Doria-Rose, Nicole A; Schramm, Chaim A; Gorman, Jason et al. (2014) Developmental pathway for potent V1V2-directed HIV-neutralizing antibodies. Nature 509:55-62|
|Tong, Tommy; Crooks, Ema T; Osawa, Keiko et al. (2014) Multi-parameter exploration of HIV-1 virus-like particles as neutralizing antibody immunogens in guinea pigs, rabbits and macaques. Virology 456-457:55-69|
|Li, Shuzhao; Rouphael, Nadine; Duraisingham, Sai et al. (2014) Molecular signatures of antibody responses derived from a systems biology study of five human vaccines. Nat Immunol 15:195-204|
|Gitlin, Alexander D; Shulman, Ziv; Nussenzweig, Michel C (2014) Clonal selection in the germinal centre by regulated proliferation and hypermutation. Nature 509:637-40|
|Pulendran, Bali (2014) Systems vaccinology: probing humanity's diverse immune systems with vaccines. Proc Natl Acad Sci U S A 111:12300-6|
|Bates, John T; Keefer, Christopher J; Slaughter, James C et al. (2014) Escape from neutralization by the respiratory syncytial virus-specific neutralizing monoclonal antibody palivizumab is driven by changes in on-rate of binding to the fusion protein. Virology 454-455:139-44|
|Sundling, Christopher; Zhang, Zhenhai; Phad, Ganesh E et al. (2014) Single-cell and deep sequencing of IgG-switched macaque B cells reveal a diverse Ig repertoire following immunization. J Immunol 192:3637-44|
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