Author
Listed:
- Marie Pancera
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Tongqing Zhou
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Aliaksandr Druz
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Ivelin S. Georgiev
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Cinque Soto
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Jason Gorman
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Jinghe Huang
(HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Priyamvada Acharya
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Gwo-Yu Chuang
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Gilad Ofek
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Guillaume B. E. Stewart-Jones
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Jonathan Stuckey
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Robert T. Bailer
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- M. Gordon Joyce
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Mark K. Louder
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Nancy Tumba
(Center for HIV and STIs, National Institute for Communicable Diseases of the National Health Laboratory Service (NHLS), Sandringham, Johannesburg 2131, South Africa)
- Yongping Yang
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Baoshan Zhang
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Myron S. Cohen
(Epidemiology, Microbiology and Immunology, University of North Carolina at Chapel Hill)
- Barton F. Haynes
(Duke University Human Vaccine Institute, Surgery, Pediatrics and Immunology, Duke University School of Medicine, and the Center for HIV/AIDS Vaccine Immunology-Immunogen Discovery at Duke University)
- John R. Mascola
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Lynn Morris
(Center for HIV and STIs, National Institute for Communicable Diseases of the National Health Laboratory Service (NHLS), Sandringham, Johannesburg 2131, South Africa
University of the Witwatersrand, Braamfontein, Johannesburg 2000, South Africa
Centre for the AIDS Programme of Research in South Africa (CAPRISA), University of KwaZulu-Natal, Durban 4041, South Africa)
- James B. Munro
(Yale University School of Medicine)
- Scott C. Blanchard
(Weill Cornell Medical College of Cornell University)
- Walther Mothes
(Yale University School of Medicine)
- Mark Connors
(HIV-Specific Immunity Section, Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
- Peter D. Kwong
(Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health)
Abstract
The human immunodeficiency virus type 1 (HIV-1) envelope (Env) spike, comprising three gp120 and three gp41 subunits, is a conformational machine that facilitates HIV-1 entry by rearranging from a mature unliganded state, through receptor-bound intermediates, to a post-fusion state. As the sole viral antigen on the HIV-1 virion surface, Env is both the target of neutralizing antibodies and a focus of vaccine efforts. Here we report the structure at 3.5 Å resolution for an HIV-1 Env trimer captured in a mature closed state by antibodies PGT122 and 35O22. This structure reveals the pre-fusion conformation of gp41, indicates rearrangements needed for fusion activation, and defines parameters of immune evasion and immune recognition. Pre-fusion gp41 encircles amino- and carboxy-terminal strands of gp120 with four helices that form a membrane-proximal collar, fastened by insertion of a fusion peptide-proximal methionine into a gp41-tryptophan clasp. Spike rearrangements required for entry involve opening the clasp and expelling the termini. N-linked glycosylation and sequence-variable regions cover the pre-fusion closed spike; we used chronic cohorts to map the prevalence and location of effective HIV-1-neutralizing responses, which were distinguished by their recognition of N-linked glycan and tolerance for epitope-sequence variation.
Suggested Citation
Marie Pancera & Tongqing Zhou & Aliaksandr Druz & Ivelin S. Georgiev & Cinque Soto & Jason Gorman & Jinghe Huang & Priyamvada Acharya & Gwo-Yu Chuang & Gilad Ofek & Guillaume B. E. Stewart-Jones & Jon, 2014.
"Structure and immune recognition of trimeric pre-fusion HIV-1 Env,"
Nature, Nature, vol. 514(7523), pages 455-461, October.
Handle:
RePEc:nat:nature:v:514:y:2014:i:7523:d:10.1038_nature13808
DOI: 10.1038/nature13808
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Cited by:
- Mathilde Foglierini & Pauline Nortier & Rachel Schelling & Rahel R. Winiger & Philippe Jacquet & Sijy O’Dell & Davide Demurtas & Maxmillian Mpina & Omar Lweno & Yannick D. Muller & Constantinos Petrov, 2024.
"RAIN: machine learning-based identification for HIV-1 bNAbs,"
Nature Communications, Nature, vol. 15(1), pages 1-16, December.
- Svenja Weiss & Vincenza Itri & Ruimin Pan & Xunqing Jiang & Christina C. Luo & Lynn Morris & Delphine C. Malherbe & Philip Barnette & Jeff Alexander & Xiang-Peng Kong & Nancy L. Haigwood & Ann J. Hess, 2022.
"Differential V2-directed antibody responses in non-human primates infected with SHIVs or immunized with diverse HIV vaccines,"
Nature Communications, Nature, vol. 13(1), pages 1-15, December.
- Jun Niu & Qi Wang & Wenwen Zhao & Bing Meng & Youwei Xu & Xianfang Zhang & Yi Feng & Qilian Qi & Yanling Hao & Xuan Zhang & Ying Liu & Jiangchao Xiang & Yiming Shao & Bei Yang, 2023.
"Structures and immune recognition of Env trimers from two Asia prevalent HIV-1 CRFs,"
Nature Communications, Nature, vol. 14(1), pages 1-18, December.
- Yi-Nan Zhang & Jennifer Paynter & Aleksandar Antanasijevic & Joel D. Allen & Mor Eldad & Yi-Zong Lee & Jeffrey Copps & Maddy L. Newby & Linling He & Deborah Chavez & Pat Frost & Anna Goodroe & John Du, 2023.
"Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates,"
Nature Communications, Nature, vol. 14(1), pages 1-29, December.
- Ignacio Fernández & Lasse Toftdal Dynesen & Youna Coquin & Riccardo Pederzoli & Delphine Brun & Ahmed Haouz & Antoine Gessain & Félix A. Rey & Florence Buseyne & Marija Backovic, 2023.
"The crystal structure of a simian Foamy Virus receptor binding domain provides clues about entry into host cells,"
Nature Communications, Nature, vol. 14(1), pages 1-14, December.
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