IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v14y2023i1d10.1038_s41467-023-40900-y.html
   My bibliography  Save this article

Chemoenzymatic synthesis of genetically-encoded multivalent liquid N-glycan arrays

Author

Listed:
  • Chih-Lan Lin

    (University of Alberta)

  • Mirat Sojitra

    (University of Alberta)

  • Eric J. Carpenter

    (University of Alberta)

  • Ellen S. Hayhoe

    (University of Alberta)

  • Susmita Sarkar

    (University of Alberta)

  • Elizabeth A. Volker

    (University of Alberta)

  • Chao Wang

    (The Scripps Research Institute)

  • Duong T. Bui

    (University of Alberta)

  • Loretta Yang

    (Lectenz Bio)

  • John S. Klassen

    (University of Alberta)

  • Peng Wu

    (The Scripps Research Institute)

  • Matthew S. Macauley

    (University of Alberta
    University of Alberta)

  • Todd L. Lowary

    (University of Alberta
    Academia Sinica
    National Taiwan University)

  • Ratmir Derda

    (University of Alberta)

Abstract

Cellular glycosylation is characterized by chemical complexity and heterogeneity, which is challenging to reproduce synthetically. Here we show chemoenzymatic synthesis on phage to produce a genetically-encoded liquid glycan array (LiGA) of complex type N-glycans. Implementing the approach involved by ligating an azide-containing sialylglycosyl-asparagine to phage functionalized with 50–1000 copies of dibenzocyclooctyne. The resulting intermediate can be trimmed by glycosidases and extended by glycosyltransferases yielding a phage library with different N-glycans. Post-reaction analysis by MALDI-TOF MS allows rigorous characterization of N-glycan structure and mean density, which are both encoded in the phage DNA. Use of this LiGA with fifteen glycan-binding proteins, including CD22 or DC-SIGN on cells, reveals optimal structure/density combinations for recognition. Injection of the LiGA into mice identifies glycoconjugates with structures and avidity necessary for enrichment in specific organs. This work provides a quantitative evaluation of the interaction of complex N-glycans with GBPs in vitro and in vivo.

Suggested Citation

  • Chih-Lan Lin & Mirat Sojitra & Eric J. Carpenter & Ellen S. Hayhoe & Susmita Sarkar & Elizabeth A. Volker & Chao Wang & Duong T. Bui & Loretta Yang & John S. Klassen & Peng Wu & Matthew S. Macauley & , 2023. "Chemoenzymatic synthesis of genetically-encoded multivalent liquid N-glycan arrays," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40900-y
    DOI: 10.1038/s41467-023-40900-y
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-023-40900-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-023-40900-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. Jennie Grace Briard & Hao Jiang & Kelley W. Moremen & Matthew Scott Macauley & Peng Wu, 2018. "Cell-based glycan arrays for probing glycan–glycan binding protein interactions," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
    2. Edward N. Schmidt & Dimitra Lamprinaki & Kelli A. McCord & Maju Joe & Mirat Sojitra & Ayk Waldow & Jasmine Nguyen & John Monyror & Elena N. Kitova & Fahima Mozaneh & Xue Yan Guo & Jaesoo Jung & Jhon R, 2023. "Siglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    3. Emily Rodrigues & Jaesoo Jung & Heajin Park & Caleb Loo & Sepideh Soukhtehzari & Elena N. Kitova & Fahima Mozaneh & Gour Daskhan & Edward N. Schmidt & Vivian Aghanya & Susmita Sarkar & Laura Streith &, 2020. "A versatile soluble siglec scaffold for sensitive and quantitative detection of glycan ligands," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
    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. Maria Pia Lenza & Leire Egia-Mendikute & Asier Antoñana-Vildosola & Cátia O. Soares & Helena Coelho & Francisco Corzana & Alexandre Bosch & Prodhi Manisha & Jon Imanol Quintana & Iker Oyenarte & Luca , 2023. "Structural insights into Siglec-15 reveal glycosylation dependency for its interaction with T cells through integrin CD11b," Nature Communications, Nature, vol. 14(1), pages 1-14, December.
    2. Edward N. Schmidt & Dimitra Lamprinaki & Kelli A. McCord & Maju Joe & Mirat Sojitra & Ayk Waldow & Jasmine Nguyen & John Monyror & Elena N. Kitova & Fahima Mozaneh & Xue Yan Guo & Jaesoo Jung & Jhon R, 2023. "Siglec-6 mediates the uptake of extracellular vesicles through a noncanonical glycolipid binding pocket," Nature Communications, Nature, vol. 14(1), pages 1-17, 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:14:y:2023:i:1:d:10.1038_s41467-023-40900-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.