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.

Public Health Relevance

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.

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project with Complex Structure Cooperative Agreement (UM1)
Project #
5UM1AI100663-02
Application #
8508853
Study Section
Special Emphasis Panel (ZAI1-JBS-A)
Project Start
Project End
Budget Start
2013-07-01
Budget End
2014-06-30
Support Year
2
Fiscal Year
2013
Total Cost
$295,027
Indirect Cost
$48,526
Name
Scripps Research Institute
Department
Type
DUNS #
781613492
City
La Jolla
State
CA
Country
United States
Zip Code
92037
Watanabe, Yasunori; Raghwani, Jayna; Allen, Joel D et al. (2018) Structure of the Lassa virus glycan shield provides a model for immunological resistance. Proc Natl Acad Sci U S A 115:7320-7325
Allen, Joel D; Sanders, Rogier W; Doores, Katie J et al. (2018) Harnessing post-translational modifications for next-generation HIV immunogens. Biochem Soc Trans 46:691-698
Gautam, Rajeev; Nishimura, Yoshiaki; Gaughan, Natalie et al. (2018) A single injection of crystallizable fragment domain-modified antibodies elicits durable protection from SHIV infection. Nat Med 24:610-616
Young, Gavin; Hundt, Nikolas; Cole, Daniel et al. (2018) Quantitative mass imaging of single biological macromolecules. Science 360:423-427
Dosenovic, Pia; Kara, Ervin E; Pettersson, Anna-Klara et al. (2018) Anti-HIV-1 B cell responses are dependent on B cell precursor frequency and antigen-binding affinity. Proc Natl Acad Sci U S A 115:4743-4748
Richard, Jonathan; Prévost, Jérémie; Baxter, Amy E et al. (2018) Uninfected Bystander Cells Impact the Measurement of HIV-Specific Antibody-Dependent Cellular Cytotoxicity Responses. MBio 9:
Abbott, Robert K; Lee, Jeong Hyun; Menis, Sergey et al. (2018) Precursor Frequency and Affinity Determine B Cell Competitive Fitness in Germinal Centers, Tested with Germline-Targeting HIV Vaccine Immunogens. Immunity 48:133-146.e6
Pauthner, Matthias G; Nkolola, Joseph P; Havenar-Daughton, Colin et al. (2018) Vaccine-Induced Protection from Homologous Tier 2 SHIV Challenge in Nonhuman Primates Depends on Serum-Neutralizing Antibody Titers. Immunity :
Lu, Ching-Lan; Pai, Joy A; Nogueira, Lilian et al. (2018) Relationship between intact HIV-1 proviruses in circulating CD4+ T cells and rebound viruses emerging during treatment interruption. Proc Natl Acad Sci U S A 115:E11341-E11348
Walker, Laura M; Burton, Dennis R (2018) Passive immunotherapy of viral infections: 'super-antibodies' enter the fray. Nat Rev Immunol 18:297-308

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