IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v12y2021i1d10.1038_s41467-021-23506-0.html
   My bibliography  Save this article

Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer

Author

Listed:
  • Martin Obr

    (Institute of Science and Technology (IST) Austria)

  • Clifton L. Ricana

    (University of Missouri)

  • Nadia Nikulin

    (Cornell University)

  • Jon-Philip R. Feathers

    (Cornell University)

  • Marco Klanschnig

    (Institute of Science and Technology (IST) Austria)

  • Andreas Thader

    (Institute of Science and Technology (IST) Austria)

  • Marc C. Johnson

    (University of Missouri)

  • Volker M. Vogt

    (Cornell University)

  • Florian K. M. Schur

    (Institute of Science and Technology (IST) Austria)

  • Robert A. Dick

    (Cornell University)

Abstract

Inositol hexakisphosphate (IP6) is an assembly cofactor for HIV-1. We report here that IP6 is also used for assembly of Rous sarcoma virus (RSV), a retrovirus from a different genus. IP6 is ~100-fold more potent at promoting RSV mature capsid protein (CA) assembly than observed for HIV-1 and removal of IP6 in cells reduces infectivity by 100-fold. Here, visualized by cryo-electron tomography and subtomogram averaging, mature capsid-like particles show an IP6-like density in the CA hexamer, coordinated by rings of six lysines and six arginines. Phosphate and IP6 have opposing effects on CA in vitro assembly, inducing formation of T = 1 icosahedrons and tubes, respectively, implying that phosphate promotes pentamer and IP6 hexamer formation. Subtomogram averaging and classification optimized for analysis of pleomorphic retrovirus particles reveal that the heterogeneity of mature RSV CA polyhedrons results from an unexpected, intrinsic CA hexamer flexibility. In contrast, the CA pentamer forms rigid units organizing the local architecture. These different features of hexamers and pentamers determine the structural mechanism to form CA polyhedrons of variable shape in mature RSV particles.

Suggested Citation

  • Martin Obr & Clifton L. Ricana & Nadia Nikulin & Jon-Philip R. Feathers & Marco Klanschnig & Andreas Thader & Marc C. Johnson & Volker M. Vogt & Florian K. M. Schur & Robert A. Dick, 2021. "Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer," Nature Communications, Nature, vol. 12(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-23506-0
    DOI: 10.1038/s41467-021-23506-0
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-021-23506-0
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-021-23506-0?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
    ---><---

    Citations

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


    Cited by:

    1. Anna-Sophia Krebs & Hsuan-Fu Liu & Ye Zhou & Juan S. Rey & Lev Levintov & Juan Shen & Andrew Howe & Juan R. Perilla & Alberto Bartesaghi & Peijun Zhang, 2023. "Molecular architecture and conservation of an immature human endogenous retrovirus," Nature Communications, Nature, vol. 14(1), pages 1-11, 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_s41467-021-23506-0. 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.