This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Vishwanath, S Articles by Ramphal, R Search for Related Content PubMed PubMed Citation Articles by Vishwanath, S Articles by Ramphal, R

 Previous Article  |  Next Article 

Infect Immun. 1985 May; 48(2): 331-335

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

ABSTRACT

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.

This article has been cited by other articles:

• Verastegui, M., Gilman, R. H., Arana, Y., Barber, D., Velasquez, J., Farfan, M., Chile, N., Kosek, J. C., Kosek, M., Garcia, H. H., Gonzalez, A., and the Cysticercosis Working Group in Peru, (2007). Taenia solium Oncosphere Adhesion to Intestinal Epithelial and Chinese Hamster Ovary Cells In Vitro. Infect. Immun. 75: 5158-5166 [Abstract] [Full Text]  
• Ryan, P. A., Pancholi, V., Fischetti, V. A. (2001). Group A Streptococci Bind to Mucin and Human Pharyngeal Cells through Sialic Acid-Containing Receptors. Infect. Immun. 69: 7402-7412 [Abstract] [Full Text]  
• Scharfman, A., Arora, S. K., Delmotte, P., Van Brussel, E., Mazurier, J., Ramphal, R., Roussel, P. (2001). Recognition of Lewis x Derivatives Present on Mucins by Flagellar Components of Pseudomonas aeruginosa. Infect. Immun. 69: 5243-5248 [Abstract] [Full Text]  
• PILEWSKI, J. M., FRIZZELL, R. A. (1999). Role of CFTR in Airway Disease. Physiol. Rev. 79: 215-255 [Abstract] [Full Text]  
• Wilson, R., Dowling, R. B (1998). Pseudomonas aeruginosa and other related species. Thorax 53: 213-219 [Full Text]