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

Pablo Gallego, Maria-Jose Garcia-Bonete, Sergio Trillo-Muyo, Christian V. Recktenwald, Malin E. V. Johansson and Gunnar C. Hansson ()
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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

Nature Communications, 2023, vol. 14, issue 1, 1-9

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-37666-8

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