Completeness of HIV-1 Envelope Glycan Shield at Transmission Determines Neutralization Breadth

Wagh, Kshitij; Kreider, Edward F.; Li, Yingying; Barbian, Hannah J.; Learn, Gerald H.; Giorgi, Elena; Hraber, Peter T.; Decker, Timothy G.; Smith, Andrew G.; Gondim, Marcos V.; Gillis, Lindsey; Wandzilak, Jamie; Chuang, Gwo-Yu; Rawi, Reda; Cai, Fangping; Pellegrino, Pierre; Williams, Ian; Overbaugh, Julie; Gao, Feng; Kwong, Peter D.; Haynes, Barton F.; Shaw, George M.; Borrow, Persephone; Seaman, Michael S.; Hahn, Beatrice H.; Korber, Bette

doi:10.1016/j.celrep.2018.09.087

Title: Completeness of HIV-1 Envelope Glycan Shield at Transmission Determines Neutralization Breadth

Journal Article · 30 September 2018 · Cell Reports

DOI: https://doi.org/10.1016/j.celrep.2018.09.087 · OSTI ID:1623646

Wagh, Kshitij ^[1]; Kreider, Edward F. ^[2]; Li, Yingying ^[2]; Barbian, Hannah J. ^[2]; Learn, Gerald H. ^[2]; Giorgi, Elena ^[3]; Hraber, Peter T. ^[3]; Decker, Timothy G. ^[2]; Smith, Andrew G. ^[2]; Gondim, Marcos V. ^[2]; Gillis, Lindsey ^[4]; Wandzilak, Jamie ^[4]; Chuang, Gwo-Yu ^[5]; Rawi, Reda ^[5]; Cai, Fangping ^[6]; Pellegrino, Pierre ^[7]; Williams, Ian ^[7]; Overbaugh, Julie ^[8]; Gao, Feng ^[6]; Kwong, Peter D. ^[5] more »

Los Alamos National Lab. (LANL), Los Alamos, NM (United States). Theoretical Biology & Biophysics; DOE/OSTI
Univ. of Pennsylvania, Philadelphia, PA (United States). Perelman School of Medicine
Los Alamos National Lab. (LANL), Los Alamos, NM (United States). Theoretical Biology & Biophysics
Center for Virology and Vaccine Research, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA (United States)
National Institutes of Health (NIH), Vaccine Research Center, Bethesda, MD (United States)
Duke Univ., Durham, NC (United States). School of Medicine, Duke Human Vaccine Institute
Center for Sexual Health & HIV Research, Mortimer Market Centre, London (United Kingdom)
Fred Hutchinson Cancer Research Center, Seattle, WA (United States). Human Biology Division
University of Oxford, Oxford (United Kingdom). Nuffield Department of Clinical Medicine

Densely arranged N-linked glycans shield the HIV-1 envelope (Env) trimer from antibody recognition. Strain-specific breaches in this shield (glycan holes) can be targets of vaccine-induced neutralizing antibodies that lack breadth. To understand the interplay between glycan holes and neutralization breadth in HIV-1 infection, we developed a sequence- and structure-based approach to identify glycan holes for individual Env sequences that are shielded in most M-group viruses. Applying this approach to 12 longitudinally followed individuals, we found that transmitted viruses with more intact glycan shields correlated with development of greater neutralization breadth. Within 2 years, glycan acquisition filled most glycan holes present at transmission, indicating escape from hole-targeting neutralizing antibodies. Glycan hole filling generally preceded the time to first detectable breadth, although time intervals varied across hosts. Thus, completely glycan-shielded viruses were associated with accelerated neutralization breadth development, suggesting that Env immunogens with intact glycan shields may be preferred components of AIDS vaccines.

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Research Organization:: Los Alamos National Lab (LANL), Los Alamos, NM (United States)

Sponsoring Organization:: Duke Center for HIV/AIDS Vaccine Immunology-Immunogen Discovery; National Institutes of Health (NIH); USDOE National Nuclear Security Administration (NNSA)

Grant/Contract Number:: AC52-06NA25396

OSTI ID:: 1623646

Journal Information:: Cell Reports, Journal Name: Cell Reports Journal Issue: 4 Vol. 25; ISSN 2211-1247

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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Consistent elicitation of cross-clade HIV-neutralizing responses achieved in guinea pigs after fusion peptide priming by repetitive envelope trimer boosting Cheng, Cheng; Xu, Kai; Kong, Rui PLOS ONE, Vol. 14, Issue 4 https://doi.org/10.1371/journal.pone.0215163	journal	April 2019
Dendritic Cells, the Double Agent in the War Against HIV-1 Martín-Moreno, Alba; Muñoz-Fernández, Mª Angeles Frontiers in Immunology, Vol. 10 https://doi.org/10.3389/fimmu.2019.02485	journal	October 2019
Field-Based Affinity Optimization of a Novel Azabicyclohexane Scaffold HIV-1 Entry Inhibitor Meuser, Megan E.; Rashad, Adel A.; Ozorowski, Gabriel Molecules, Vol. 24, Issue 8 https://doi.org/10.3390/molecules24081581	journal	April 2019

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