6OZC

BG505 SOSIP.664 with 2G12 Fab2

Summary for 6OZC

• Entry DOI: 10.2210/pdb6ozc/pdb
• EMDB information: 20224
• Descriptor: Envelope glycoprotein gp160, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (12 entities in total)
• Functional Keywords: hiv env, viral protein
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 18
• Total formula weight: 527754.78

Authors

Cottrell, C.A.,Ward, A.B. (deposition date: 2019-05-15, release date: 2020-05-20, Last modification date: 2024-11-06)

Primary citation

Seabright, G.E.,Cottrell, C.A.,van Gils, M.J.,D'addabbo, A.,Harvey, D.J.,Behrens, A.J.,Allen, J.D.,Watanabe, Y.,Scaringi, N.,Polveroni, T.M.,Maker, A.,Vasiljevic, S.,de Val, N.,Sanders, R.W.,Ward, A.B.,Crispin, M.
Networks of HIV-1 Envelope Glycans Maintain Antibody Epitopes in the Face of Glycan Additions and Deletions.
Structure, 28:897-, 2020

PubMed Abstract: Numerous broadly neutralizing antibodies (bnAbs) have been identified that target the glycans of the HIV-1 envelope spike. Neutralization breadth is notable given that glycan processing can be substantially influenced by the presence or absence of neighboring glycans. Here, using a stabilized recombinant envelope trimer, we investigate the degree to which mutations in the glycan network surrounding an epitope impact the fine glycan processing of antibody targets. Using cryo-electron microscopy and site-specific glycan analysis, we reveal the importance of glycans in the formation of the 2G12 bnAb epitope and show that the epitope is only subtly impacted by variations in the glycan network. In contrast, we show that the PG9 and PG16 glycan-based epitopes at the trimer apex are dependent on the presence of the highly conserved surrounding glycans. Glycan networks underpin the conservation of bnAb epitopes and are an important parameter in immunogen design.

PubMed: 32433992
DOI: 10.1016/j.str.2020.04.022

Experimental method

ELECTRON MICROSCOPY (3.79 Å)