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Mechanism of cooperative N-glycan processing by the multi-modular endoglycosidase EndoE

Author

Listed:
  • Mikel García-Alija

    (Cruces University Hospital
    Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park)

  • Jonathan J. Du

    (Emory University School of Medicine)

  • Izaskun Ordóñez

    (Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park)

  • Asier Diz-Vallenilla

    (Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park)

  • Alicia Moraleda-Montoya

    (Cruces University Hospital
    Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park)

  • Nazneen Sultana

    (Emory University School of Medicine)

  • Chau G. Huynh

    (Emory University School of Medicine)

  • Chao Li

    (University of Maryland)

  • Thomas Connor Donahue

    (University of Maryland)

  • Lai-Xi Wang

    (University of Maryland)

  • Beatriz Trastoy

    (Cruces University Hospital
    Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park)

  • Eric J. Sundberg

    (Emory University School of Medicine)

  • Marcelo E. Guerin

    (Cruces University Hospital
    Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), Bizkaia Technology Park
    Ikerbasque, Basque Foundation for Science)

Abstract

Bacteria produce a remarkably diverse range of glycoside hydrolases to metabolize glycans from the environment as a primary source of nutrients, and to promote the colonization and infection of a host. Here we focus on EndoE, a multi-modular glycoside hydrolase secreted by Enterococcus faecalis, one of the leading causes of healthcare-associated infections. We provide X-ray crystal structures of EndoE, which show an architecture composed of four domains, including GH18 and GH20 glycoside hydrolases connected by two consecutive three α-helical bundles. We determine that the GH20 domain is an exo-β-1,2-N-acetylglucosaminidase, whereas the GH18 domain is an endo-β-1,4-N-acetylglucosaminidase that exclusively processes the central core of complex-type or high-mannose-type N-glycans. Both glycoside hydrolase domains act in a concerted manner to process diverse N-glycans on glycoproteins, including therapeutic IgG antibodies. EndoE combines two enzyme domains with distinct functions and glycan specificities to play a dual role in glycan metabolism and immune evasion.

Suggested Citation

  • 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.
  • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28722-w
    DOI: 10.1038/s41467-022-28722-w
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    References listed on IDEAS

    as
    1. 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.
    2. Beatriz Trastoy & Erik Klontz & Jared Orwenyo & Alberto Marina & Lai-Xi Wang & Eric J. Sundberg & Marcelo E. Guerin, 2018. "Structural basis for the recognition of complex-type N-glycans by Endoglycosidase S," Nature Communications, Nature, vol. 9(1), pages 1-11, December.
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    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. Abigail S. L. Sudol & John Butler & Dylan P. Ivory & Ivo Tews & Max Crispin, 2022. "Extensive substrate recognition by the streptococcal antibody-degrading enzymes IdeS and EndoS," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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