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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Luzina, Irina G. Hyun, Sang Won Liu, Anguo Atamas, Sergei P. Goldblum, Simeon E. Guang, Wei Lillehoj, Erik P. Verceles, Avelino C. Kim, K. Chul |
| Description | Author Affiliation: Lillehoj EP ( From the Departments of Pediatrics.); Hyun SW ( Medicine, and.); Liu A ( Medicine, and.); Guang W ( From the Departments of Pediatrics.); Verceles AC ( Medicine, and.); Luzina IG ( Medicine, and the Baltimore Veterans Affairs Medical Center, Baltimore, Maryland 21201, and.); Atamas SP ( Medicine, and the Baltimore Veterans Affairs Medical Center, Baltimore, Maryland 21201, and.); Kim KC ( the Department of Otolaryngology, University of Arizona College of Medicine, Tucson, Arizona 85724.); Goldblum SE ( Medicine, and the Baltimore Veterans Affairs Medical Center, Baltimore, Maryland 21201, and Pathology, University of Maryland School of Medicine, Baltimore, Maryland 21201, sgoldblu@mbrc.umaryland.edu.) |
| 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. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 30 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-07-24 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Flagellin Metabolism Lung Mucin-1 Neuraminidase Pseudomonas Aeruginosa Adhesins, Bacterial Bacterial Adhesion Bronchoalveolar Lavage Fluid Cell Line Microbiology Pathology N-Acetylneuraminic Acid Protein Binding Protein Structure, Tertiary Pathogenicity Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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