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7L85

Designed tetrahedral nanoparticle T33-31 presenting BG505 SOSIP trimers

Summary for 7L85
Entry DOI10.2210/pdb7l85/pdb
EMDB information23222
DescriptorBG505 SOSIP-T33-31B, BG505 SOSIP-T33-31A (2 entities in total)
Functional Keywordshiv, vaccine design, protein design, nanoparticles, bg505, viral protein, de novo protein
Biological sourceHuman immunodeficiency virus 1 (HIV-1)
More
Total number of polymer chains24
Total formula weight304537.52
Authors
Antanasijevic, A.,Sewall, L.M.,Ward, A.B. (deposition date: 2020-12-31, release date: 2021-08-04, Last modification date: 2024-05-29)
Primary citationAntanasijevic, A.,Sewall, L.M.,Cottrell, C.A.,Carnathan, D.G.,Jimenez, L.E.,Ngo, J.T.,Silverman, J.B.,Groschel, B.,Georgeson, E.,Bhiman, J.,Bastidas, R.,LaBranche, C.,Allen, J.D.,Copps, J.,Perrett, H.R.,Rantalainen, K.,Cannac, F.,Yang, Y.R.,de la Pena, A.T.,Rocha, R.F.,Berndsen, Z.T.,Baker, D.,King, N.P.,Sanders, R.W.,Moore, J.P.,Crotty, S.,Crispin, M.,Montefiori, D.C.,Burton, D.R.,Schief, W.R.,Silvestri, G.,Ward, A.B.
Polyclonal antibody responses to HIV Env immunogens resolved using cryoEM.
Nat Commun, 12:4817-4817, 2021
Cited by
PubMed Abstract: Engineered ectodomain trimer immunogens based on BG505 envelope glycoprotein are widely utilized as components of HIV vaccine development platforms. In this study, we used rhesus macaques to evaluate the immunogenicity of several stabilized BG505 SOSIP constructs both as free trimers and presented on a nanoparticle. We applied a cryoEM-based method for high-resolution mapping of polyclonal antibody responses elicited in immunized animals (cryoEMPEM). Mutational analysis coupled with neutralization assays were used to probe the neutralization potential at each epitope. We demonstrate that cryoEMPEM data can be used for rapid, high-resolution analysis of polyclonal antibody responses without the need for monoclonal antibody isolation. This approach allowed to resolve structurally distinct classes of antibodies that bind overlapping sites. In addition to comprehensive mapping of commonly targeted neutralizing and non-neutralizing epitopes in BG505 SOSIP immunogens, our analysis revealed that epitopes comprising engineered stabilizing mutations and of partially occupied glycosylation sites can be immunogenic.
PubMed: 34376662
DOI: 10.1038/s41467-021-25087-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.9 Å)
Structure validation

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