6NQD

Cryo-EM structure of T/F100 SOSIP.664 HIV-1 Env trimer in complex with 8ANC195 Fab

Summary for 6NQD

• Entry DOI: 10.2210/pdb6nqd/pdb
• EMDB information: 0485
• Descriptor: T/F100 Env gp120, 2-acetamido-2-deoxy-beta-D-glucopyranose, T/F100 Env gp41, ... (10 entities in total)
• Functional Keywords: hiv-1, env, trimer, viral protein-immune system complex, viral protein/immune system
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 12
• Total formula weight: 401996.83

Authors

Fang, Q.,Rossmann, M.G. (deposition date: 2019-01-21, release date: 2019-03-06, Last modification date: 2024-10-16)

Primary citation

Ananthaswamy, N.,Fang, Q.,AlSalmi, W.,Jain, S.,Chen, Z.,Klose, T.,Sun, Y.,Liu, Y.,Mahalingam, M.,Chand, S.,Tovanabutra, S.,Robb, M.L.,Rossmann, M.G.,Rao, V.B.
A sequestered fusion peptide in the structure of an HIV-1 transmitted founder envelope trimer.
Nat Commun, 10:873-873, 2019

PubMed Abstract: The envelope protein of human immunodeficiency virus-1 (HIV-1) and its fusion peptide are essential for cell entry and vaccine design. Here, we describe the 3.9-Å resolution structure of an envelope protein trimer from a very early transmitted founder virus (CRF01_AE T/F100) complexed with Fab from the broadly neutralizing antibody (bNAb) 8ANC195. The overall T/F100 trimer structure is similar to other reported "closed" state prefusion trimer structures. In contrast, the fusion peptide, which is exposed to solvent in reported closed structures, is sequestered (buried) in the hydrophobic core of the T/F100 trimer. A buried conformation has previously been observed in "open" state structures formed after CD4 receptor binding. The T/F100 trimer binds poorly to bNAbs including the fusion peptide-specific bNAbs PGT151 and VRC34.01. The T/F100 structure might represent a prefusion state, intermediate between the closed and open states. These observations are relevant to mechanisms of HIV-1 transmission and vaccine design.

PubMed: 30787293
DOI: 10.1038/s41467-019-08825-7

Experimental method

ELECTRON MICROSCOPY (3.9 Å)