ArticleThe Journal of biological chemistry2015
NEU1 Sialidase Regulates Membrane-tethered Mucin (MUC1) Ectodomain Adhesiveness for Pseudomonas aeruginosa and Decoy Receptor Release.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
23 citing papers in PubMed, 1 synthesis or guideline pooled it, 37 citations in OpenAlex.
- Mammalian Neuraminidases in Immune-Mediated Diseases: Mucins and Beyond.Frontiers in immunology · 2022Pooled it
- Deglycosylation at War: Host N-Glycoprotein Remodeling in Infection and Immunity.Infection and drug resistance · 2026Review
- Article
- The role of sialidase Neu1 in respiratory diseases.Respiratory research · 2024Review
- Lung bronchiectasisas a paradigm of the interplay between infection and colonization on plastic modulation of the pre-metastatic niche.Frontiers in oncology · 2024Article
- Co-infection of the respiratory epithelium, scene of complex functional interactions between viral, bacterial, and human neuraminidases.Frontiers in microbiology · 2023Review
- Sialidase Inhibitors with Different Mechanisms.Journal of medicinal chemistry · 2022Review
- MUC1 ectodomain is a flagellin-targeting decoy receptor and biomarker operative during Pseudomonas aeruginosa lung infection.Scientific reports · 2021Article
- Membrane-associated mucins of the human ocular surface in health and disease.The ocular surface · 2021Review
- Sialylation of host proteins as targetable risk factor for COVID-19 susceptibility and spreading: A hypothesis.FASEB bioAdvances · 2021Article
- Therapeutic Effect of Neuraminidase-1-Selective Inhibition in Mouse Models of Bleomycin-Induced Pulmonary Inflammation and Fibrosis.The Journal of pharmacology and experimental therapeutics · 2021Article
- Contact lens-related corneal infection: Intrinsic resistance and its compromise.Progress in retinal and eye research · 2020Review
- Sialidase NEU1 suppresses progression of human bladder cancer cells by inhibiting fibronectin-integrin α5β1 interaction and Akt signaling pathway.Cell communication and signaling : CCS · 2020Article
- Article
- Membrane-associated mucins of the ocular surface: New genes, new protein functions and new biological roles in human and mouse.Progress in retinal and eye research · 2020Review
- Neuraminidase 1-mediated desialylation of the mucin 1 ectodomain releases a decoy receptor that protects againstThe Journal of biological chemistry · 2019Article
- The structure of PilA fromThe Journal of biological chemistry · 2019Article
- The Role of the Cell Surface Mucin MUC1 as a Barrier to Infection and Regulator of Inflammation.Frontiers in cellular and infection microbiology · 2019Review
- MUC1: The First Respiratory Mucin with an Anti-Inflammatory Function.Journal of clinical medicine · 2017Review
- The cell surface mucin MUC1 limits the severity of influenza A virus infection.Mucosal immunology · 2017Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
Abstract
Airway epithelia express sialylated receptors that recognize exogenous danger signals. Regulation of receptor responsiveness to these signals remains incompletely defined. Here, we explore the mechanisms through which the human sialidase, neuraminidase-1 (NEU1), promotes the interaction between the sialoprotein, mucin 1 (MUC1), and the opportunistic pathogen, Pseudomonas aeruginosa. P. aeruginosa flagellin engaged the MUC1 ectodomain (ED), increasing NEU1 association with MUC1. The flagellin stimulus increased the association of MUC1-ED with both NEU1 and its chaperone/transport protein, protective protein/cathepsin A. Scatchard analysis demonstrated NEU1-dependent increased binding affinity of flagellin to MUC1-expressing epithelia. NEU1-driven MUC1-ED desialylation rapidly increased P. aeruginosa adhesion to and invasion of the airway epithelium. MUC1-ED desialylation also increased its shedding, and the shed MUC1-ED competitively blocked P. aeruginosa adhesion to cell-associated MUC1-ED. Levels of desialylated MUC1-ED were elevated in the bronchoalveolar lavage fluid of mechanically ventilated patients with P. aeruginosa airway colonization. Preincubation of P. aeruginosa with these same ex vivo fluids competitively inhibited bacterial adhesion to airway epithelia, and MUC1-ED immunodepletion completely abrogated their inhibitory activity. These data indicate that a prokaryote, P. aeruginosa, in a ligand-specific manner, mobilizes eukaryotic NEU1 to enhance bacterial pathogenicity, but the host retaliates by releasing MUC1-ED into the airway lumen as a hyperadhesive decoy receptor.
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Registered trials
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