6XRT

Cryo-EM structure of SHIV-elicited RHA1.V2.01 in complex with HIV-1 Env BG505 DS-SOSIP.664

Summary for 6XRT

• Entry DOI: 10.2210/pdb6xrt/pdb
• EMDB information: 22295
• Descriptor: Envelope glycoprotein gp160, 2-acetamido-2-deoxy-beta-D-glucopyranose, HIV-1 Envelope Glycoprotein BG505 SOSIP.664 gp41, ... (10 entities in total)
• Functional Keywords: shiv, v1v2, v2-apex, sosip, vaccine, pgt145, immune system, immune system-viral protein complex, immune system/viral protein
• Biological source: Human immunodeficiency virus 1; More
• Total number of polymer chains: 8
• Total formula weight: 257736.03

Authors

Gorman, J.,Kwong, P.D. (deposition date: 2020-07-13, release date: 2020-10-07, Last modification date: 2024-10-30)

Primary citation

Roark, R.S.,Li, H.,Williams, W.B.,Chug, H.,Mason, R.D.,Gorman, J.,Wang, S.,Lee, F.H.,Rando, J.,Bonsignori, M.,Hwang, K.K.,Saunders, K.O.,Wiehe, K.,Moody, M.A.,Hraber, P.T.,Wagh, K.,Giorgi, E.E.,Russell, R.M.,Bibollet-Ruche, F.,Liu, W.,Connell, J.,Smith, A.G.,DeVoto, J.,Murphy, A.I.,Smith, J.,Ding, W.,Zhao, C.,Chohan, N.,Okumura, M.,Rosario, C.,Ding, Y.,Lindemuth, E.,Bauer, A.M.,Bar, K.J.,Ambrozak, D.,Chao, C.W.,Chuang, G.Y.,Geng, H.,Lin, B.C.,Louder, M.K.,Nguyen, R.,Zhang, B.,Lewis, M.G.,Raymond, D.D.,Doria-Rose, N.A.,Schramm, C.A.,Douek, D.C.,Roederer, M.,Kepler, T.B.,Kelsoe, G.,Mascola, J.R.,Kwong, P.D.,Korber, B.T.,Harrison, S.C.,Haynes, B.F.,Hahn, B.H.,Shaw, G.M.
Recapitulation of HIV-1 Env-antibody coevolution in macaques leading to neutralization breadth.
Science, 371:-, 2021

PubMed Abstract: Neutralizing antibodies elicited by HIV-1 coevolve with viral envelope proteins (Env) in distinctive patterns, in some cases acquiring substantial breadth. We report that primary HIV-1 envelope proteins-when expressed by simian-human immunodeficiency viruses in rhesus macaques-elicited patterns of Env-antibody coevolution very similar to those in humans, including conserved immunogenetic, structural, and chemical solutions to epitope recognition and precise Env-amino acid substitutions, insertions, and deletions leading to virus persistence. The structure of one rhesus antibody, capable of neutralizing 49% of a 208-strain panel, revealed a V2 apex mode of recognition like that of human broadly neutralizing antibodies (bNAbs) PGT145 and PCT64-35S. Another rhesus antibody bound the CD4 binding site by CD4 mimicry, mirroring human bNAbs 8ANC131, CH235, and VRC01. Virus-antibody coevolution in macaques can thus recapitulate developmental features of human bNAbs, thereby guiding HIV-1 immunogen design.

PubMed: 33214287
DOI: 10.1126/science.abd2638

Experimental method

ELECTRON MICROSCOPY (3.9 Å)