6MAR
HIV-1 Envelope Glycoprotein Clone BG505 delCT N332T in complex with broadly neutralizing antibody Fab PGT151
Summary for 6MAR
Entry DOI | 10.2210/pdb6mar/pdb |
EMDB information | 9062 |
Descriptor | Immunoglobulin G PGT151 Fab, Heavy chain, 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, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (13 entities in total) |
Functional Keywords | fusion protein-fab complex, membrane protein |
Biological source | Homo sapiens More |
Total number of polymer chains | 10 |
Total formula weight | 366670.05 |
Authors | Berndsen, Z.T.,Ward, A.B. (deposition date: 2018-08-28, release date: 2018-09-26, Last modification date: 2020-07-29) |
Primary citation | Cao, L.,Pauthner, M.,Andrabi, R.,Rantalainen, K.,Berndsen, Z.,Diedrich, J.K.,Menis, S.,Sok, D.,Bastidas, R.,Park, S.R.,Delahunty, C.M.,He, L.,Guenaga, J.,Wyatt, R.T.,Schief, W.R.,Ward, A.B.,Yates, J.R.,Burton, D.R.,Paulson, J.C. Differential processing of HIV envelope glycans on the virus and soluble recombinant trimer. Nat Commun, 9:3693-3693, 2018 Cited by PubMed Abstract: As the sole target of broadly neutralizing antibodies (bnAbs) to HIV, the envelope glycoprotein (Env) trimer is the focus of vaccination strategies designed to elicit protective bnAbs in humans. Because HIV Env is densely glycosylated with 75-90 N-glycans per trimer, most bnAbs use or accommodate them in their binding epitope, making the glycosylation of recombinant Env a key aspect of HIV vaccine design. Upon analysis of three HIV strains, we here find that site-specific glycosylation of Env from infectious virus closely matches Envs from corresponding recombinant membrane-bound trimers. However, viral Envs differ significantly from recombinant soluble, cleaved (SOSIP) Env trimers, strongly impacting antigenicity. These results provide a benchmark for virus Env glycosylation needed for the design of soluble Env trimers as part of an overall HIV vaccine strategy. PubMed: 30209313DOI: 10.1038/s41467-018-06121-4 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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