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An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability. / van Gils, Marit J.; van den Kerkhof, Tom L. G. M.; Ozorowski, Gabriel et al.

In: Nature microbiology, Vol. 2, No. 2, 2016, p. 16199.

Research output: Contribution to journalArticleAcademicpeer-review

Harvard

van Gils, MJ, van den Kerkhof, TLGM, Ozorowski, G, Cottrell, CA, Sok, D, Pauthner, M, Pallesen, J, de Val, N, Yasmeen, A, de Taeye, SW, Schorcht, A, Gumbs, S, Johanna, I, Saye-Francisco, K, Liang, C-H, Landais, E, Nie, X, Pritchard, LK, Crispin, M, Kelsoe, G, Wilson, IA, Schuitemaker, H, Klasse, PJ, Moore, JP, Burton, DR, Ward, AB & Sanders, RW 2016, 'An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability', Nature microbiology, vol. 2, no. 2, pp. 16199. https://doi.org/10.1038/nmicrobiol.2016.199

APA

van Gils, M. J., van den Kerkhof, T. L. G. M., Ozorowski, G., Cottrell, C. A., Sok, D., Pauthner, M., Pallesen, J., de Val, N., Yasmeen, A., de Taeye, S. W., Schorcht, A., Gumbs, S., Johanna, I., Saye-Francisco, K., Liang, C-H., Landais, E., Nie, X., Pritchard, L. K., Crispin, M., ... Sanders, R. W. (2016). An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability. Nature microbiology, 2(2), 16199. https://doi.org/10.1038/nmicrobiol.2016.199

Vancouver

van Gils MJ, van den Kerkhof TLGM, Ozorowski G, Cottrell CA, Sok D, Pauthner M et al. An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability. Nature microbiology. 2016;2(2):16199. doi: 10.1038/nmicrobiol.2016.199

Author

BibTeX

@article{9eb2068157c84ce1a9a97119ca9b0b2f,
title = "An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability",
abstract = "The induction by vaccination of broadly neutralizing antibodies (bNAbs) capable of neutralizing various HIV-1 viral strains is challenging, but understanding how a subset of HIV-infected individuals develops bNAbs may guide immunization strategies. Here, we describe the isolation and characterization of the bNAb ACS202 from an elite neutralizer that recognizes a new, trimer-specific and cleavage-dependent epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 and the gp41 fusion peptide. In addition, an Env trimer, AMC011 SOSIP.v4.2, based on early virus isolates from the same elite neutralizer, was constructed, and its structure by cryo-electron microscopy at 6.2 {\AA} resolution reveals a closed, pre-fusion conformation similar to that of the BG505 SOSIP.664 trimer. The availability of a native-like Env trimer and a bNAb from the same elite neutralizer provides the opportunity to design vaccination strategies aimed at generating similar bNAbs against a key functional site on HIV-1",
author = "{van Gils}, {Marit J.} and {van den Kerkhof}, {Tom L. G. M.} and Gabriel Ozorowski and Cottrell, {Christopher A.} and Devin Sok and Matthias Pauthner and Jesper Pallesen and {de Val}, Natalia and Anila Yasmeen and {de Taeye}, {Steven W.} and Anna Schorcht and Stephanie Gumbs and Inez Johanna and Karen Saye-Francisco and Chi-Hui Liang and Elise Landais and Xiaoyan Nie and Pritchard, {Laura K.} and Max Crispin and Garnett Kelsoe and Wilson, {Ian A.} and Hanneke Schuitemaker and Klasse, {Per Johan} and Moore, {John P.} and Burton, {Dennis R.} and Ward, {Andrew B.} and Sanders, {Rogier W.}",
year = "2016",
doi = "10.1038/nmicrobiol.2016.199",
language = "English",
volume = "2",
pages = "16199",
journal = "Nature microbiology",
issn = "2058-5276",
publisher = "Nature Publishing Group",
number = "2",

}

RIS

TY - JOUR

T1 - An HIV-1 antibody from an elite neutralizer implicates the fusion peptide as a site of vulnerability

AU - van Gils, Marit J.

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

AU - Ozorowski, Gabriel

AU - Cottrell, Christopher A.

AU - Sok, Devin

AU - Pauthner, Matthias

AU - Pallesen, Jesper

AU - de Val, Natalia

AU - Yasmeen, Anila

AU - de Taeye, Steven W.

AU - Schorcht, Anna

AU - Gumbs, Stephanie

AU - Johanna, Inez

AU - Saye-Francisco, Karen

AU - Liang, Chi-Hui

AU - Landais, Elise

AU - Nie, Xiaoyan

AU - Pritchard, Laura K.

AU - Crispin, Max

AU - Kelsoe, Garnett

AU - Wilson, Ian A.

AU - Schuitemaker, Hanneke

AU - Klasse, Per Johan

AU - Moore, John P.

AU - Burton, Dennis R.

AU - Ward, Andrew B.

AU - Sanders, Rogier W.

PY - 2016

Y1 - 2016

N2 - The induction by vaccination of broadly neutralizing antibodies (bNAbs) capable of neutralizing various HIV-1 viral strains is challenging, but understanding how a subset of HIV-infected individuals develops bNAbs may guide immunization strategies. Here, we describe the isolation and characterization of the bNAb ACS202 from an elite neutralizer that recognizes a new, trimer-specific and cleavage-dependent epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 and the gp41 fusion peptide. In addition, an Env trimer, AMC011 SOSIP.v4.2, based on early virus isolates from the same elite neutralizer, was constructed, and its structure by cryo-electron microscopy at 6.2 Å resolution reveals a closed, pre-fusion conformation similar to that of the BG505 SOSIP.664 trimer. The availability of a native-like Env trimer and a bNAb from the same elite neutralizer provides the opportunity to design vaccination strategies aimed at generating similar bNAbs against a key functional site on HIV-1

AB - The induction by vaccination of broadly neutralizing antibodies (bNAbs) capable of neutralizing various HIV-1 viral strains is challenging, but understanding how a subset of HIV-infected individuals develops bNAbs may guide immunization strategies. Here, we describe the isolation and characterization of the bNAb ACS202 from an elite neutralizer that recognizes a new, trimer-specific and cleavage-dependent epitope at the gp120-gp41 interface of the envelope glycoprotein (Env), involving the glycan N88 and the gp41 fusion peptide. In addition, an Env trimer, AMC011 SOSIP.v4.2, based on early virus isolates from the same elite neutralizer, was constructed, and its structure by cryo-electron microscopy at 6.2 Å resolution reveals a closed, pre-fusion conformation similar to that of the BG505 SOSIP.664 trimer. The availability of a native-like Env trimer and a bNAb from the same elite neutralizer provides the opportunity to design vaccination strategies aimed at generating similar bNAbs against a key functional site on HIV-1

U2 - 10.1038/nmicrobiol.2016.199

DO - 10.1038/nmicrobiol.2016.199

M3 - Article

C2 - 27841852

VL - 2

SP - 16199

JO - Nature microbiology

JF - Nature microbiology

SN - 2058-5276

IS - 2

ER -

ID: 3018301