Tracheobronchial mucin receptor for Pseudomonas aeruginosa: predominance of amino sugars in binding sites.

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Pseudomonas aeruginosa, a common respiratory tract colonizer and pathogen, adheres to injured tracheal cells and to tracheobronchial mucin. These phenomena suggest that there are specific receptors for this organism in the respiratory tract. The receptor on injured tracheal cells contains n-acetylneuraminic acid as the principal sugar, but the structure of the receptor in mucin has not been described. Using a microtiter plate assay to study bacterial adherence to mucin, we have partially characterized the mucin receptor for P. aeruginosa. The receptor for both nonmucoid and mucoid strains is sensitive to periodate oxidation, suggesting that it is carbohydrate in nature, and the amino sugars n-acetylglucosamine and n-acetylneuraminic acid inhibited the adherence of both types of strains. Nonmucoid strains were more sensitive to inhibition by n-acetylneuraminic acid than to inhibition by n-acetylglucosamine, but the mucoid strains varied in their sensitivities to inhibition by each amino sugar. Preincubation of mucin with heat-inactivated influenza A virus (which binds to neuraminic acid) significantly reduced the adherence of P. aeruginosa. Treatment of mucin with Clostridium perfringens neuraminidase also reduced bacterial adherence significantly. Treatment of mucin with pronase did not affect adherence. Our results suggest that n-acetylglucosamine and n-acetylneuraminic acid are important constituents of the binding sites for P. aeruginosa on human tracheobronchial mucin.

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