Contrast Variation SANS Experiments to Differentiate Shape Profile of Glyco- and Protein-Part of HIV-1 gp141 Envelope Trimer -/+ CD4 or mAb
Being a heavily glycosylated protein in its native state, HIV-1 gp120/41 envelope protein is still poorly understood by biophysical methods. Since it is key to both viral entry and replication, and a candidate for practical vaccine against HIV-1, clear understanding of how it is folded and binds to its receptor CD4 or antibodies is highly sought. By acquiring SANS data at different deuteration contrast points, we aim to resolve which portions of trimeric assembly are sugar and protein and how they are correlated in shape. Also, data will be obtained to refine what shape changes occur in solution when the protein core opens-up to bind receptor or antibody. These are first of their kind experiments, and any success would be a big achievement in structural biology of HIV entry mechanism or vaccine design understanding.
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SAGAR Amin; ASHISH Ashish; BERNADO Pau and PORCAR Lionel. (2020). Contrast Variation SANS Experiments to Differentiate Shape Profile of Glyco- and Protein-Part of HIV-1 gp141 Envelope Trimer -/+ CD4 or mAb. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-997
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