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Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike

Author

Listed:
  • Gabriel Ozorowski

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

  • Jesper Pallesen

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

  • Natalia de Val

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute
    NanoImaging Services)

  • Dmitry Lyumkis

    (Laboratory of Genetics and Helmsley Center for Genomic Medicine, The Salk Institute for Biological Studies)

  • Christopher A. Cottrell

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

  • Jonathan L. Torres

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

  • Jeffrey Copps

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

  • Robyn L. Stanfield

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

  • Albert Cupo

    (Weill Medical College of Cornell University)

  • Pavel Pugach

    (Weill Medical College of Cornell University)

  • John P. Moore

    (Weill Medical College of Cornell University)

  • Ian A. Wilson

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute
    The Skaggs Institute for Chemical Biology, The Scripps Research Institute)

  • Andrew B. Ward

    (Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, International AIDS Vaccine Initiative Neutralizing Antibody Center, and Collaboration for AIDS Vaccine Discovery, The Scripps Research Institute)

Abstract

New high-resolution cryo-electron microscopy structures of the HIV-1 envelope protein provide a detailed description and understanding of how the HIV-1 fusion machinery functions and how it changes its structure over time to convert from the pre-fusion to the fusion-intermediate conformation.

Suggested Citation

  • Gabriel Ozorowski & Jesper Pallesen & Natalia de Val & Dmitry Lyumkis & Christopher A. Cottrell & Jonathan L. Torres & Jeffrey Copps & Robyn L. Stanfield & Albert Cupo & Pavel Pugach & John P. Moore &, 2017. "Open and closed structures reveal allostery and pliability in the HIV-1 envelope spike," Nature, Nature, vol. 547(7663), pages 360-363, July.
    • Handle: RePEc:nat:nature:v:547:y:2017:i:7663:d:10.1038_nature23010
    DOI: 10.1038/nature23010
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    Cited by:

    1. Daniel Ellis & Julia Lederhofer & Oliver J. Acton & Yaroslav Tsybovsky & Sally Kephart & Christina Yap & Rebecca A. Gillespie & Adrian Creanga & Audrey Olshefsky & Tyler Stephens & Deleah Pettie & Mic, 2022. "Structure-based design of stabilized recombinant influenza neuraminidase tetramers," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Durgadevi Parthasarathy & Karunakar Reddy Pothula & Sneha Ratnapriya & Héctor Cervera Benet & Ruth Parsons & Xiao Huang & Salam Sammour & Katarzyna Janowska & Miranda Harris & Joseph Sodroski & Priyam, 2024. "Conformational flexibility of HIV-1 envelope glycoproteins modulates transmitted/founder sensitivity to broadly neutralizing antibodies," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Zhi Yang & Kim-Marie A. Dam & Michael D. Bridges & Magnus A. G. Hoffmann & Andrew T. DeLaitsch & Harry B. Gristick & Amelia Escolano & Rajeev Gautam & Malcolm A. Martin & Michel C. Nussenzweig & Wayne, 2022. "Neutralizing antibodies induced in immunized macaques recognize the CD4-binding site on an occluded-open HIV-1 envelope trimer," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    4. Shixia Wang & Kun-Wei Chan & Danlan Wei & Xiuwen Ma & Shuying Liu & Guangnan Hu & Saeyoung Park & Ruimin Pan & Ying Gu & Alexandra F. Nazzari & Adam S. Olia & Kai Xu & Bob C. Lin & Mark K. Louder & Kr, 2024. "Human CD4-binding site antibody elicited by polyvalent DNA prime-protein boost vaccine neutralizes cross-clade tier-2-HIV strains," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    5. Xandra Nuqui & Lorenzo Casalino & Ling Zhou & Mohamed Shehata & Albert Wang & Alexandra L. Tse & Anupam A. Ojha & Fiona L. Kearns & Mia A. Rosenfeld & Emily Happy Miller & Cory M. Acreman & Surl-Hee A, 2024. "Simulation-driven design of stabilized SARS-CoV-2 spike S2 immunogens," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    6. 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.
    7. Jinliang Guo & Shangrong Li & Lisha Bai & Huimin Zhao & Wenyu Shang & Zhaojun Zhong & Tuerxunjiang Maimaiti & Xueyan Gao & Ning Ji & Yanjie Chao & Zhaofei Li & Dijun Du, 2024. "Structural transition of GP64 triggered by a pH-sensitive multi-histidine switch," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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