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A sequestered fusion peptide in the structure of an HIV-1 transmitted founder envelope trimer

Author

Listed:
  • Neeti Ananthaswamy

    (The Catholic University of America)

  • Qianglin Fang

    (Purdue University)

  • Wadad AlSalmi

    (The Catholic University of America)

  • Swati Jain

    (The Catholic University of America)

  • Zhenguo Chen

    (Purdue University
    Fudan University)

  • Thomas Klose

    (Purdue University)

  • Yingyuan Sun

    (Purdue University)

  • Yue Liu

    (Purdue University)

  • Marthandan Mahalingam

    (The Catholic University of America)

  • Subhash Chand

    (The Catholic University of America)

  • Sodsai Tovanabutra

    (Henry M. Jackson Foundation for the Advancement of Military Medicine)

  • Merlin L. Robb

    (Henry M. Jackson Foundation for the Advancement of Military Medicine)

  • Michael G. Rossmann

    (Purdue University)

  • Venigalla B. Rao

    (The Catholic University of America)

Abstract

The envelope protein of human immunodeficiency virus-1 (HIV-1) and its fusion peptide are essential for cell entry and vaccine design. Here, we describe the 3.9-Å resolution structure of an envelope protein trimer from a very early transmitted founder virus (CRF01_AE T/F100) complexed with Fab from the broadly neutralizing antibody (bNAb) 8ANC195. The overall T/F100 trimer structure is similar to other reported “closed” state prefusion trimer structures. In contrast, the fusion peptide, which is exposed to solvent in reported closed structures, is sequestered (buried) in the hydrophobic core of the T/F100 trimer. A buried conformation has previously been observed in “open” state structures formed after CD4 receptor binding. The T/F100 trimer binds poorly to bNAbs including the fusion peptide-specific bNAbs PGT151 and VRC34.01. The T/F100 structure might represent a prefusion state, intermediate between the closed and open states. These observations are relevant to mechanisms of HIV-1 transmission and vaccine design.

Suggested Citation

  • Neeti Ananthaswamy & Qianglin Fang & Wadad AlSalmi & Swati Jain & Zhenguo Chen & Thomas Klose & Yingyuan Sun & Yue Liu & Marthandan Mahalingam & Subhash Chand & Sodsai Tovanabutra & Merlin L. Robb & M, 2019. "A sequestered fusion peptide in the structure of an HIV-1 transmitted founder envelope trimer," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08825-7
    DOI: 10.1038/s41467-019-08825-7
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    Cited by:

    1. Jérémie Prévost & Yaozong Chen & Fei Zhou & William D. Tolbert & Romain Gasser & Halima Medjahed & Manon Nayrac & Dung N. Nguyen & Suneetha Gottumukkala & Ann J. Hessell & Venigalla B. Rao & Edwin Poz, 2023. "Structure-function analyses reveal key molecular determinants of HIV-1 CRF01_AE resistance to the entry inhibitor temsavir," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. 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.

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