IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-16165-0.html
   My bibliography  Save this article

Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein

Author

Listed:
  • Alessandro Piai

    (Harvard Medical School)

  • Qingshan Fu

    (Harvard Medical School)

  • Yongfei Cai

    (Boston Children’s Hospital
    Harvard Medical School)

  • Fadi Ghantous

    (Beth Israel Deaconess Medical Center)

  • Tianshu Xiao

    (Boston Children’s Hospital
    Harvard Medical School)

  • Md Munan Shaik

    (Boston Children’s Hospital
    Harvard Medical School)

  • Hanqin Peng

    (Boston Children’s Hospital)

  • Sophia Rits-Volloch

    (Boston Children’s Hospital)

  • Wen Chen

    (Harvard Medical School)

  • Michael S. Seaman

    (Beth Israel Deaconess Medical Center)

  • Bing Chen

    (Boston Children’s Hospital
    Harvard Medical School)

  • James J. Chou

    (Harvard Medical School)

Abstract

The prefusion conformation of HIV-1 envelope protein (Env) is recognized by most broadly neutralizing antibodies (bnAbs). Studies showed that alterations of its membrane-related components, including the transmembrane domain (TMD) and cytoplasmic tail (CT), can reshape the antigenic structure of the Env ectodomain. Using nuclear magnetic resonance (NMR) spectroscopy, we determine the structure of an Env segment encompassing the TMD and a large portion of the CT in bicelles. The structure reveals that the CT folds into amphipathic helices that wrap around the C-terminal end of the TMD, thereby forming a support baseplate for the rest of Env. NMR dynamics measurements provide evidences of dynamic coupling across the TMD between the ectodomain and CT. Pseudovirus-based neutralization assays suggest that CT-TMD interaction preferentially affects antigenic structure near the apex of the Env trimer. These results explain why the CT can modulate the Env antigenic properties and may facilitate HIV-1 Env-based vaccine design.

Suggested Citation

  • Alessandro Piai & Qingshan Fu & Yongfei Cai & Fadi Ghantous & Tianshu Xiao & Md Munan Shaik & Hanqin Peng & Sophia Rits-Volloch & Wen Chen & Michael S. Seaman & Bing Chen & James J. Chou, 2020. "Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein," Nature Communications, Nature, vol. 11(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16165-0
    DOI: 10.1038/s41467-020-16165-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-16165-0
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-16165-0?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-16165-0. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.