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Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo. / Medina-Ramírez, Max; Garces, Fernando; Escolano, Amelia et al.

In: Journal of experimental medicine, Vol. 214, No. 9, 2017, p. 2573-2590.

Research output: Contribution to journalArticleAcademicpeer-review

Harvard

Medina-Ramírez, M, Garces, F, Escolano, A, Skog, P, de Taeye, SW, del Moral-Sanchez, I, McGuire, AT, Yasmeen, A, Behrens, A-J, Ozorowski, G, van den Kerkhof, TLGM, Freund, NT, Dosenovic, P, Hua, Y, Gitlin, AD, Cupo, A, van der Woude, P, Golabek, M, Sliepen, K, Blane, T, Kootstra, N, van Breemen, MJ, Pritchard, LK, Stanfield, RL, Crispin, M, Ward, AB, Stamatatos, L, Klasse, PJ, Moore, JP, Nemazee, D, Nussenzweig, MC, Wilson, IA & Sanders, RW 2017, 'Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo', Journal of experimental medicine, vol. 214, no. 9, pp. 2573-2590. https://doi.org/10.1084/jem.20161160

APA

Medina-Ramírez, M., Garces, F., Escolano, A., Skog, P., de Taeye, S. W., del Moral-Sanchez, I., McGuire, A. T., Yasmeen, A., Behrens, A-J., Ozorowski, G., van den Kerkhof, T. L. G. M., Freund, N. T., Dosenovic, P., Hua, Y., Gitlin, A. D., Cupo, A., van der Woude, P., Golabek, M., Sliepen, K., ... Sanders, R. W. (2017). Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo. Journal of experimental medicine, 214(9), 2573-2590. https://doi.org/10.1084/jem.20161160

Vancouver

Medina-Ramírez M, Garces F, Escolano A, Skog P, de Taeye SW, del Moral-Sanchez I et al. Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo. Journal of experimental medicine. 2017;214(9):2573-2590. doi: 10.1084/jem.20161160

Author

Medina-Ramírez, Max ; Garces, Fernando ; Escolano, Amelia et al. / Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo. In: Journal of experimental medicine. 2017 ; Vol. 214, No. 9. pp. 2573-2590.

BibTeX

@article{24484c615da8464d854538eee7092ac0,
title = "Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo",
abstract = "Induction of broadly neutralizing antibodies (bNAbs) by HIV-1 envelope glycoprotein immunogens would be a major advance toward an effective vaccine. A critical step in this process is the activation of naive B cells expressing germline (gl) antibody precursors that have the potential to evolve into bNAbs. Here, we reengineered the BG505 SOSIP.664 glycoprotein to engage gl precursors of bNAbs that target either the trimer apex or the CD4-binding site. The resulting BG505 SOSIP.v4.1-GT1 trimer binds multiple bNAb gl precursors in vitro. Immunization experiments in knock-in mice expressing gl-VRC01 or gl-PGT121 show that this trimer activates B cells in vivo, resulting in the secretion of specific antibodies into the sera. A crystal structure of the gl-targeting trimer at 3.2-{\AA} resolution in complex with neutralizing antibodies 35O22 and 9H+109L reveals a native-like conformation and the successful incorporation of design features associated with binding of multiple gl-bNAb precursors",
author = "Max Medina-Ram{\'i}rez and Fernando Garces and Amelia Escolano and Patrick Skog and {de Taeye}, {Steven W.} and {del Moral-Sanchez}, Ivan and McGuire, {Andrew T.} and Anila Yasmeen and Anna-Janina Behrens and Gabriel Ozorowski and {van den Kerkhof}, {Tom L. G. M.} and Freund, {Natalia T.} and Pia Dosenovic and Yuanzi Hua and Gitlin, {Alexander D.} and Albert Cupo and {van der Woude}, Patricia and Michael Golabek and Kwinten Sliepen and Tanya Blane and Neeltje Kootstra and {van Breemen}, {Mari{\"e}lle J.} and Pritchard, {Laura K.} and Stanfield, {Robyn L.} and Max Crispin and Ward, {Andrew B.} and Leonidas Stamatatos and Klasse, {Per Johan} and Moore, {John P.} and David Nemazee and Nussenzweig, {Michel C.} and Wilson, {Ian A.} and Sanders, {Rogier W.}",
year = "2017",
doi = "10.1084/jem.20161160",
language = "English",
volume = "214",
pages = "2573--2590",
journal = "Journal of experimental medicine",
issn = "0022-1007",
publisher = "Rockefeller University Press",
number = "9",

}

RIS

TY - JOUR

T1 - Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo

AU - Medina-Ramírez, Max

AU - Garces, Fernando

AU - Escolano, Amelia

AU - Skog, Patrick

AU - de Taeye, Steven W.

AU - del Moral-Sanchez, Ivan

AU - McGuire, Andrew T.

AU - Yasmeen, Anila

AU - Behrens, Anna-Janina

AU - Ozorowski, Gabriel

AU - van den Kerkhof, Tom L. G. M.

AU - Freund, Natalia T.

AU - Dosenovic, Pia

AU - Hua, Yuanzi

AU - Gitlin, Alexander D.

AU - Cupo, Albert

AU - van der Woude, Patricia

AU - Golabek, Michael

AU - Sliepen, Kwinten

AU - Blane, Tanya

AU - Kootstra, Neeltje

AU - van Breemen, Mariëlle J.

AU - Pritchard, Laura K.

AU - Stanfield, Robyn L.

AU - Crispin, Max

AU - Ward, Andrew B.

AU - Stamatatos, Leonidas

AU - Klasse, Per Johan

AU - Moore, John P.

AU - Nemazee, David

AU - Nussenzweig, Michel C.

AU - Wilson, Ian A.

AU - Sanders, Rogier W.

PY - 2017

Y1 - 2017

N2 - Induction of broadly neutralizing antibodies (bNAbs) by HIV-1 envelope glycoprotein immunogens would be a major advance toward an effective vaccine. A critical step in this process is the activation of naive B cells expressing germline (gl) antibody precursors that have the potential to evolve into bNAbs. Here, we reengineered the BG505 SOSIP.664 glycoprotein to engage gl precursors of bNAbs that target either the trimer apex or the CD4-binding site. The resulting BG505 SOSIP.v4.1-GT1 trimer binds multiple bNAb gl precursors in vitro. Immunization experiments in knock-in mice expressing gl-VRC01 or gl-PGT121 show that this trimer activates B cells in vivo, resulting in the secretion of specific antibodies into the sera. A crystal structure of the gl-targeting trimer at 3.2-Å resolution in complex with neutralizing antibodies 35O22 and 9H+109L reveals a native-like conformation and the successful incorporation of design features associated with binding of multiple gl-bNAb precursors

AB - Induction of broadly neutralizing antibodies (bNAbs) by HIV-1 envelope glycoprotein immunogens would be a major advance toward an effective vaccine. A critical step in this process is the activation of naive B cells expressing germline (gl) antibody precursors that have the potential to evolve into bNAbs. Here, we reengineered the BG505 SOSIP.664 glycoprotein to engage gl precursors of bNAbs that target either the trimer apex or the CD4-binding site. The resulting BG505 SOSIP.v4.1-GT1 trimer binds multiple bNAb gl precursors in vitro. Immunization experiments in knock-in mice expressing gl-VRC01 or gl-PGT121 show that this trimer activates B cells in vivo, resulting in the secretion of specific antibodies into the sera. A crystal structure of the gl-targeting trimer at 3.2-Å resolution in complex with neutralizing antibodies 35O22 and 9H+109L reveals a native-like conformation and the successful incorporation of design features associated with binding of multiple gl-bNAb precursors

U2 - 10.1084/jem.20161160

DO - 10.1084/jem.20161160

M3 - Article

C2 - 28847869

VL - 214

SP - 2573

EP - 2590

JO - Journal of experimental medicine

JF - Journal of experimental medicine

SN - 0022-1007

IS - 9

ER -

ID: 4058345