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J Proteome Res. 2018 Mar 2;17(3):987-999. doi: 10.1021/acs.jproteome.7b00639. Epub 2018 Feb 8.

Integrity of Glycosylation Processing of a Glycan-Depleted Trimeric HIV-1 Immunogen Targeting Key B-Cell Lineages.

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Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford , South Parks Road, Oxford OX1 3QU, United Kingdom.
Laboratory of Experimental Virology, Department of Medical Microbiology, Center for Infection and Immunity Amsterdam (CINIMA), Academic Medical Center of the University of Amsterdam , 1105 AZ Amsterdam, The Netherlands.
Department of Microbiology and Immunology, Weill Cornell Medical College, New York , New York, New York 10021, United States.
Department of Integrative Structural and Computational Biology, IAVI Neutralizing Antibody Center and CAVD, Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute , La Jolla, California 92037, United States.
Skaggs Institute for Chemical Biology, The Scripps Research Institute , La Jolla, California 92037, United States.
Centre for Biological Sciences and Institute for Life Sciences, University of Southampton , Southampton SO17 1BJ, United Kingdom.


Broadly neutralizing antibodies (bNAbs) that target the trimeric HIV-1 envelope glycoprotein spike (Env) are tools that can guide the design of recombinant Env proteins intended to engage the predicted human germline precursors of bNAbs (gl-bNAbs). The protein components of gl-bNAb epitopes are often masked by glycans, while mature bNAbs can evolve to accommodate or bypass these shielding glycans. The design of germline-targeting Env immunogens therefore includes the targeted deletion of specific glycan sites. However, the processing of glycans on Env trimers can be influenced by the density with which they are packed together, a highly relevant point given the essential contributions under-processed glycans make to multiple bNAb epitopes. We sought to determine the impact of the removal of 15 potential N-glycan sites (5 per protomer) from the germline-targeting soluble trimer, BG505 SOSIP.v4.1-GT1, using quantitative, site-specific N-glycan mass spectrometry analysis. We find that, compared with SOSIP.664, there was little overall change in the glycan profile but only subtle increases in the extent of processing at sites immediately adjacent to where glycans had been deleted. We conclude that multiple glycans can be deleted from BG505 SOSIP trimers without perturbing the overall integrity of the glycan shield.


Env; HIV-1 vaccine design; envelope; glycoproteomics; glycosylation; immunogen design; mass spectrometry; virus

[Available on 2019-03-02]
[Indexed for MEDLINE]

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