IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-14754-7.html
   My bibliography  Save this article

Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides

Author

Listed:
  • Beatriz Trastoy

    (Bizkaia Technology Park)

  • Jonathan J. Du

    (University of Maryland School of Medicine
    Emory University School of Medicine)

  • Erik H. Klontz

    (University of Maryland School of Medicine
    University of Maryland School of Medicine
    University of Maryland School of Medicine)

  • Chao Li

    (University of Maryland)

  • Javier O. Cifuente

    (Bizkaia Technology Park)

  • Lai-Xi Wang

    (University of Maryland)

  • Eric J. Sundberg

    (University of Maryland School of Medicine
    University of Maryland School of Medicine
    University of Maryland School of Medicine
    Emory University School of Medicine)

  • Marcelo E. Guerin

    (Bizkaia Technology Park
    IKERBASQUE, Basque Foundation for Science)

Abstract

The human gut microbiota plays a central role not only in regulating the metabolism of nutrients but also promoting immune homeostasis, immune responses and protection against pathogen colonization. The genome of the Gram-negative symbiont Bacteroides thetaiotaomicron, a dominant member of the human intestinal microbiota, encodes polysaccharide utilization loci PULs, the apparatus required to orchestrate the degradation of a specific glycan. EndoBT-3987 is a key endo-β-N-acetylglucosaminidase (ENGase) that initiates the degradation/processing of mammalian high-mannose-type (HM-type) N-glycans in the intestine. Here, we provide structural snapshots of EndoBT-3987, including the unliganded form, the EndoBT-3987-Man9GlcNAc2Asn substrate complex, and two EndoBT-3987-Man9GlcNAc and EndoBT-3987-Man5GlcNAc product complexes. In combination with alanine scanning mutagenesis and activity measurements we unveil the molecular mechanism of HM-type recognition and specificity for EndoBT-3987 and an important group of the GH18 ENGases, including EndoH, an enzyme extensively used in biotechnology, and for which the mechanism of substrate recognition was largely unknown.

Suggested Citation

  • Beatriz Trastoy & Jonathan J. Du & Erik H. Klontz & Chao Li & Javier O. Cifuente & Lai-Xi Wang & Eric J. Sundberg & Marcelo E. Guerin, 2020. "Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14754-7
    DOI: 10.1038/s41467-020-14754-7
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-14754-7
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-020-14754-7?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. Beatriz Trastoy & Jonathan J. Du & Javier O. Cifuente & Lorena Rudolph & Mikel García-Alija & Erik H. Klontz & Daniel Deredge & Nazneen Sultana & Chau G. Huynh & Maria W. Flowers & Chao Li & Diego E. , 2023. "Mechanism of antibody-specific deglycosylation and immune evasion by Streptococcal IgG-specific endoglycosidases," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    2. Mikel García-Alija & Jonathan J. Du & Izaskun Ordóñez & Asier Diz-Vallenilla & Alicia Moraleda-Montoya & Nazneen Sultana & Chau G. Huynh & Chao Li & Thomas Connor Donahue & Lai-Xi Wang & Beatriz Trast, 2022. "Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE," Nature Communications, Nature, vol. 13(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:11:y:2020:i:1:d:10.1038_s41467-020-14754-7. 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.