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. 2021 Nov 22;11:22725. doi: 10.1038/s41598-021-02242-x

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© The Author(s) 2021

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Pa-expressed flagellin provokes NEU1-mediated MUC1-ED desialylation to generate a flagellin-targeting MUC1-ED decoy receptor. The Pa flagellin subunit engages cell-associated MUC1-ED (step 1), leading to recruitment of a preformed pool of intracellular NEU1, together with its chaperone protein, PPCA, to MUC1-ED (step 2). NEU1 desialylates the MUC1-ED (step 3), to increase its adhesiveness for Pa (step 4) and unmask its glycine-serine (Gly-Ser) protease recognition site (step 5), permitting sheddase-mediated MUC1-ED release from the airway EC surface (step 6). Shed, desialylated MUC1-ED in the airway lumen acts as a soluble decoy receptor that reduces Pa motility, competitively inhibits Pa adhesion to cell-associated MUC1-ED and subsequent invasion of airway epithelia, protects against Pa biofilm formation, and enhances Pa phagocytosis by host PMNs (step 7).