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Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G

Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G
Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G

Summary 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.

0092-8674
813-826
Stewart-Jones, Guillaume B.E.
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Soto, Cinque
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Lemmin, Thomas
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Chuang, Gwo Yu
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Druz, Aliaksandr
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Kong, Rui
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Thomas, Paul V.
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Wagh, Kshitij
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Zhou, Tongqing
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Behrens, Anna Janina
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Bylund, Tatsiana
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Choi, Chang W.
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Davison, Jack R.
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Georgiev, Ivelin S.
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Joyce, M. Gordon
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Kwon, Young Do
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Pancera, Marie
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Taft, Justin
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Yang, Yongping
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Zhang, Baoshan
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Shivatare, Sachin S.
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Shivatare, Vidya S.
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Lee, Chang Chun D
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Wu, Chung Yi
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Bewley, Carole A.
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Burton, Dennis R.
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Koff, Wayne C.
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Connors, Mark
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Crispin, Max
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Baxa, Ulrich
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Korber, Bette T.
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Wong, Chi Huey
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Mascola, John R.
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Kwong, Peter D.
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Stewart-Jones, Guillaume B.E.
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Soto, Cinque
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Lemmin, Thomas
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Chuang, Gwo Yu
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Druz, Aliaksandr
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Kong, Rui
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Thomas, Paul V.
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Wagh, Kshitij
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Zhou, Tongqing
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Behrens, Anna Janina
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Bylund, Tatsiana
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Choi, Chang W.
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Davison, Jack R.
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Georgiev, Ivelin S.
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Joyce, M. Gordon
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Kwon, Young Do
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Pancera, Marie
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Taft, Justin
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Yang, Yongping
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Zhang, Baoshan
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Shivatare, Sachin S.
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Shivatare, Vidya S.
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Connors, Mark
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Crispin, Max
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Baxa, Ulrich
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Korber, Bette T.
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Wong, Chi Huey
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Mascola, John R.
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Kwong, Peter D.
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Stewart-Jones, Guillaume B.E., Soto, Cinque, Lemmin, Thomas, Chuang, Gwo Yu, Druz, Aliaksandr, Kong, Rui, Thomas, Paul V., Wagh, Kshitij, Zhou, Tongqing, Behrens, Anna Janina, Bylund, Tatsiana, Choi, Chang W., Davison, Jack R., Georgiev, Ivelin S., Joyce, M. Gordon, Kwon, Young Do, Pancera, Marie, Taft, Justin, Yang, Yongping, Zhang, Baoshan, Shivatare, Sachin S., Shivatare, Vidya S., Lee, Chang Chun D, Wu, Chung Yi, Bewley, Carole A., Burton, Dennis R., Koff, Wayne C., Connors, Mark, Crispin, Max, Baxa, Ulrich, Korber, Bette T., Wong, Chi Huey, Mascola, John R. and Kwong, Peter D. (2016) Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G. Cell, 165 (4), 813-826. (doi:10.1016/j.cell.2016.04.010).

Record type: Article

Abstract

Summary 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.

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More information

Accepted/In Press date: 1 April 2016
e-pub ahead of print date: 21 April 2016
Published date: 5 May 2016

Identifiers

Local EPrints ID: 414325
URI: http://eprints.soton.ac.uk/id/eprint/414325
ISSN: 0092-8674
PURE UUID: aea02f37-4407-4004-be53-28d168e150d2
ORCID for Max Crispin: ORCID iD orcid.org/0000-0002-1072-2694

Catalogue record

Date deposited: 26 Sep 2017 16:30
Last modified: 06 Jun 2024 01:59

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Contributors

Author: Guillaume B.E. Stewart-Jones
Author: Cinque Soto
Author: Thomas Lemmin
Author: Gwo Yu Chuang
Author: Aliaksandr Druz
Author: Rui Kong
Author: Paul V. Thomas
Author: Kshitij Wagh
Author: Tongqing Zhou
Author: Anna Janina Behrens
Author: Tatsiana Bylund
Author: Chang W. Choi
Author: Jack R. Davison
Author: Ivelin S. Georgiev
Author: M. Gordon Joyce
Author: Young Do Kwon
Author: Marie Pancera
Author: Justin Taft
Author: Yongping Yang
Author: Baoshan Zhang
Author: Sachin S. Shivatare
Author: Vidya S. Shivatare
Author: Chang Chun D Lee
Author: Chung Yi Wu
Author: Carole A. Bewley
Author: Dennis R. Burton
Author: Wayne C. Koff
Author: Mark Connors
Author: Max Crispin ORCID iD
Author: Ulrich Baxa
Author: Bette T. Korber
Author: Chi Huey Wong
Author: John R. Mascola
Author: Peter D. Kwong

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