IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v12y2021i1d10.1038_s41467-021-23533-x.html
   My bibliography  Save this article

Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1

Author

Listed:
  • Jin Chai

    (Brookhaven National Laboratory)

  • Yuanheng Cai

    (Stony Brook University)

  • Changxu Pang

    (Brookhaven National Laboratory)

  • Liguo Wang

    (Brookhaven National Laboratory)

  • Sean McSweeney

    (Brookhaven National Laboratory)

  • John Shanklin

    (Brookhaven National Laboratory
    Stony Brook University)

  • Qun Liu

    (Brookhaven National Laboratory
    Brookhaven National Laboratory)

Abstract

The COVID-19 pandemic, caused by the SARS-CoV-2 virus, has created global health and economic emergencies. SARS-CoV-2 viruses promote their own spread and virulence by hijacking human proteins, which occurs through viral protein recognition of human targets. To understand the structural basis for SARS-CoV-2 viral-host protein recognition, here we use cryo-electron microscopy (cryo-EM) to determine a complex structure of the human cell junction protein PALS1 and SARS-CoV-2 viral envelope (E) protein. Our reported structure shows that the E protein C-terminal DLLV motif recognizes a pocket formed exclusively by hydrophobic residues from the PDZ and SH3 domains of PALS1. Our structural analysis provides an explanation for the observation that the viral E protein recruits PALS1 from lung epithelial cell junctions. In addition, our structure provides novel targets for peptide- and small-molecule inhibitors that could block the PALS1-E interactions to reduce E-mediated virulence.

Suggested Citation

  • Jin Chai & Yuanheng Cai & Changxu Pang & Liguo Wang & Sean McSweeney & John Shanklin & Qun Liu, 2021. "Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1," Nature Communications, Nature, vol. 12(1), pages 1-6, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23533-x
    DOI: 10.1038/s41467-021-23533-x
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-021-23533-x
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-021-23533-x?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
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Lei Liu & Lijingyao Zhang & Xinyan Hao & Yang Wang & Xiaochun Zhang & Liang Ge & Peihui Wang & Boxue Tian & Min Zhang, 2024. "Coronavirus envelope protein activates TMED10-mediated unconventional secretion of inflammatory factors," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

    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:12:y:2021:i:1:d:10.1038_s41467-021-23533-x. 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.