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7SQ1

BG505.MD39TS Env trimer in complex with Fab from antibody C05

Summary for 7SQ1
Entry DOI10.2210/pdb7sq1/pdb
EMDB information25376
DescriptorTransmembrane protein gp41, Envelope glycoprotein gp160, C05 Fab Light chain, ... (9 entities in total)
Functional Keywordsantibody, env, envelope, viral protein-immune system complex, viral protein/immune system
Biological sourceHuman immunodeficiency virus 1
More
Total number of polymer chains10
Total formula weight282506.51
Authors
Moore, A.,Du, J.,Xu, Z.,Walker, S.,Kulp, D.W.,Pallesen, J. (deposition date: 2021-11-04, release date: 2022-06-22, Last modification date: 2024-10-30)
Primary citationXu, Z.,Walker, S.,Wise, M.C.,Chokkalingam, N.,Purwar, M.,Moore, A.,Tello-Ruiz, E.,Wu, Y.,Majumdar, S.,Konrath, K.M.,Kulkarni, A.,Tursi, N.J.,Zaidi, F.I.,Reuschel, E.L.,Patel, I.,Obeirne, A.,Du, J.,Schultheis, K.,Gites, L.,Smith, T.,Mendoza, J.,Broderick, K.E.,Humeau, L.,Pallesen, J.,Weiner, D.B.,Kulp, D.W.
Induction of tier-2 neutralizing antibodies in mice with a DNA-encoded HIV envelope native like trimer.
Nat Commun, 13:695-695, 2022
Cited by
PubMed Abstract: HIV Envelope (Env) is the main vaccine target for induction of neutralizing antibodies. Stabilizing Env into native-like trimer (NLT) conformations is required for recombinant protein immunogens to induce autologous neutralizing antibodies(nAbs) against difficult to neutralize HIV strains (tier-2) in rabbits and non-human primates. Immunizations of mice with NLTs have generally failed to induce tier-2 nAbs. Here, we show that DNA-encoded NLTs fold properly in vivo and induce autologous tier-2 nAbs in mice. DNA-encoded NLTs also uniquely induce both CD4 + and CD8 + T-cell responses as compared to corresponding protein immunizations. Murine neutralizing antibodies are identified with an advanced sequencing technology. The structure of an Env-Ab (C05) complex, as determined by cryo-EM, identifies a previously undescribed neutralizing Env C3/V5 epitope. Beyond potential functional immunity gains, DNA vaccines permit in vivo folding of structured antigens and provide significant cost and speed advantages for enabling rapid evaluation of new HIV vaccines.
PubMed: 35121758
DOI: 10.1038/s41467-022-28363-z
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.8 Å)
Structure validation

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