5FYK

Crystal Structure at 3.7 A Resolution of Fully Glycosylated HIV-1 Clade B JR-FL SOSIP.664 Prefusion Env Trimer in Complex with Broadly Neutralizing Antibodies PGT122, 35O22 and VRC01

Summary for 5FYK

• Entry DOI: 10.2210/pdb5fyk/pdb
• Related: 5FYJ 5FYL
• Descriptor: JR-FL, GP41 ENV ECTODOMAIN, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]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, ... (24 entities in total)
• Functional Keywords: viral protein, hiv, envelope, glycan, trimer
• Biological source: HUMAN IMMUNODEFICIENCY VIRUS 1; More
• Total number of polymer chains: 8
• Total formula weight: 246324.72

Authors

Stewart-Jones, G.B.E.,Zhou, T.,Thomas, P.V.,Kwong, P.D. (deposition date: 2016-03-08, release date: 2016-04-27, Last modification date: 2024-11-13)

Primary citation

Stewart-Jones, G.B.E.,Soto, C.,Lemmin, T.,Chuang, G.Y.,Druz, A.,Kong, R.,Thomas, P.V.,Wagh, K.,Zhou, T.,Behrens, A.J.,Bylund, T.,Choi, C.W.,Davison, J.R.,Georgiev, I.S.,Joyce, M.G.,Kwon, Y.D.,Pancera, M.,Taft, J.,Yang, Y.,Zhang, B.,Shivatare, S.S.,Shivatare, V.S.,Lee, C.C.D.,Wu, C.Y.,Bewley, C.A.,Burton, D.R.,Koff, W.C.,Connors, M.,Crispin, M.,Korber, B.T.,Wong, C.H.,Mascola, J.R.,Kwong, P.D.
Trimeric HIV-1-Env Structures Define Glycan Shields from Clades A, B and G
Cell(Cambridge,Mass.), 165:813-, 2016

PubMed Abstract: The HIV-1-envelope (Env) trimer is covered by a glycan shield of ∼90 N-linked oligosaccharides, which comprises roughly half its mass and is a key component of HIV evasion from humoral immunity. To understand how antibodies can overcome the barriers imposed by the glycan shield, we crystallized fully glycosylated Env trimers from clades A, B, and G, visualizing the shield at 3.4-3.7 Å resolution. These structures reveal the HIV-1-glycan shield to comprise a network of interlocking oligosaccharides, substantially ordered by glycan crowding, that encase the protein component of Env and enable HIV-1 to avoid most antibody-mediated neutralization. The revealed features delineate a taxonomy of N-linked glycan-glycan interactions. Crowded and dispersed glycans are differently ordered, conserved, processed, and recognized by antibody. The structures, along with glycan-array binding and molecular dynamics, reveal a diversity in oligosaccharide affinity and a requirement for accommodating glycans among known broadly neutralizing antibodies that target the glycan-shielded trimer.

PubMed: 27114034
DOI: 10.1016/J.CELL.2016.04.010

Experimental method

X-RAY DIFFRACTION (3.107 Å)