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The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins

Author

Listed:
  • Pablo Gallego

    (University of Gothenburg)

  • Maria-Jose Garcia-Bonete

    (University of Gothenburg)

  • Sergio Trillo-Muyo

    (University of Gothenburg)

  • Christian V. Recktenwald

    (University of Gothenburg)

  • Malin E. V. Johansson

    (University of Gothenburg)

  • Gunnar C. Hansson

    (University of Gothenburg)

Abstract

The MUC2 mucin polymer is the main building unit of the intestinal mucus layers separating intestinal microbiota from the host epithelium. The MUC2 mucin is a large glycoprotein with a C-terminal domain similar to the MUC5AC and MUC5B mucins and the von Willebrand factor (VWF). A structural model of the C-terminal part of MUC2, MUC2-C, was generated by combining Cryo-electron microscopy, AlphaFold prediction, information of its glycosylation, and small angle X-ray scattering information. The globular VWD4 assembly in the N-terminal of MUC2-C is followed by 3.5 linear VWC domains that form an extended flexible structure before the C-terminal cystine-knot. All gel-forming mucins and VWF form tail-tail disulfide-bonded dimers in their C-terminal cystine-knot domain, but interestingly the MUC2 mucin has an extra stabilizing disulfide bond on the N-terminal side of the VWD4 domain, likely essential for a stable intestinal mucus barrier.

Suggested Citation

  • Pablo Gallego & Maria-Jose Garcia-Bonete & Sergio Trillo-Muyo & Christian V. Recktenwald & Malin E. V. Johansson & Gunnar C. Hansson, 2023. "The intestinal MUC2 mucin C-terminus is stabilized by an extra disulfide bond in comparison to von Willebrand factor and other gel-forming mucins," Nature Communications, Nature, vol. 14(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-37666-8
    DOI: 10.1038/s41467-023-37666-8
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    References listed on IDEAS

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