IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v15y2024i1d10.1038_s41467-024-55034-y.html
   My bibliography  Save this article

Human ANP32A/B are SUMOylated and utilized by avian influenza virus NS2 protein to overcome species-specific restriction

Author

Listed:
  • Liuke Sun

    (The Chinese Academy of Agricultural Sciences)

  • Xing Guo

    (The Chinese Academy of Agricultural Sciences)

  • Mengmeng Yu

    (The Chinese Academy of Agricultural Sciences)

  • Xue-Feng Wang

    (The Chinese Academy of Agricultural Sciences)

  • Huiling Ren

    (The Chinese Academy of Agricultural Sciences)

  • Xiaojun Wang

    (The Chinese Academy of Agricultural Sciences
    The Chinese Academy of Agricultural Sciences)

Abstract

Human ANP32A/B (huANP32A/B) poorly support the polymerase activity of avian influenza viruses (AIVs), thereby limiting interspecies transmission of AIVs from birds to humans. The SUMO-interacting motif (SIM) within NS2 promotes the adaptation of AIV polymerase to huANP32A/B via a yet undisclosed mechanism. Here we show that huANP32A/B are SUMOylated by the E3 SUMO ligase PIAS2α, and deSUMOylated by SENP1. SUMO modification of huANP32A/B results in the recruitment of NS2, thereby facilitating huANP32A/B-supported AIV polymerase activity. Such a SUMO-dependent recruitment of NS2 is mediated by its association with huANP32A/B via the SIM-SUMO interaction module, where K68/K153-SUMO in huANP32A or K68/K116-SUMO in huANP32B interacts with the NS2-SIM. The SIM-SUMO-mediated interactions between NS2 and huANP32A/B function to promote AIV polymerase activity by positively regulating AIV vRNP-huANP32A/B interactions and AIV vRNP assembly. Our study offers insights into the mechanism of NS2-SIM in facilitating AIVs adaptation to mammals.

Suggested Citation

  • Liuke Sun & Xing Guo & Mengmeng Yu & Xue-Feng Wang & Huiling Ren & Xiaojun Wang, 2024. "Human ANP32A/B are SUMOylated and utilized by avian influenza virus NS2 protein to overcome species-specific restriction," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-55034-y
    DOI: 10.1038/s41467-024-55034-y
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-024-55034-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-024-55034-y?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
    ---><---

    References listed on IDEAS

    as
    1. Benoît Arragain & Tim Krischuns & Martin Pelosse & Petra Drncova & Martin Blackledge & Nadia Naffakh & Stephen Cusack, 2024. "Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Ecco Staller & Loïc Carrique & Olivia C. Swann & Haitian Fan & Jeremy R. Keown & Carol M. Sheppard & Wendy S. Barclay & Jonathan M. Grimes & Ervin Fodor, 2024. "Structures of H5N1 influenza polymerase with ANP32B reveal mechanisms of genome replication and host adaptation," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    3. Benjamin Mänz & Linda Brunotte & Peter Reuther & Martin Schwemmle, 2012. "Adaptive mutations in NEP compensate for defective H5N1 RNA replication in cultured human cells," Nature Communications, Nature, vol. 3(1), pages 1-11, January.
    Full references (including those not matched with items on IDEAS)

    Most related items

    These are the items that most often cite the same works as this one and are cited by the same works as this one.
    1. Franziska Günl & Tim Krischuns & Julian A. Schreiber & Lea Henschel & Marius Wahrenburg & Hannes C. A. Drexler & Sebastian A. Leidel & Vlad Cojocaru & Guiscard Seebohm & Alexander Mellmann & Martin Sc, 2023. "The ubiquitination landscape of the influenza A virus polymerase," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Alewo Idoko-Akoh & Daniel H. Goldhill & Carol M. Sheppard & Dagmara Bialy & Jessica L. Quantrill & Ksenia Sukhova & Jonathan C. Brown & Samuel Richardson & Ciara Campbell & Lorna Taylor & Adrian Sherm, 2023. "Creating resistance to avian influenza infection through genome editing of the ANP32 gene family," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Sharmada Swaminath & Marisa Mendes & Yipeng Zhang & Kaleigh A. Remick & Isabel Mejia & Melissa Güereca & Aartjan J. W. Velthuis & Alistair B. Russell, 2025. "Analysis of NS2-dependent effects on influenza PB1 segment extends replication requirements beyond the canonical promoter," Nature Communications, Nature, vol. 16(1), pages 1-15, December.
    4. Benoît Arragain & Tim Krischuns & Martin Pelosse & Petra Drncova & Martin Blackledge & Nadia Naffakh & Stephen Cusack, 2024. "Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase," Nature Communications, Nature, vol. 15(1), pages 1-20, 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:15:y:2024:i:1:d:10.1038_s41467-024-55034-y. 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.

    If CitEc recognized a bibliographic reference but did not link an item in RePEc to it, you can help with 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.