Abstract
Colonization of the respiratory tract with Pseudomonas aeruginosa is a serious problem in cystic fibrosis and seriously ill hospitalized patients. Human tracheobronchial mucin (HTBM), the major glycoprotein of human tracheobronchial secretions, is known to interact with this pathogen, which may then be cleared by mucociliary action. However, the mechanism of interaction is not known. To understand this process, pure HTBM was isolated from tracheobronchial secretions of a laryngectomee. Following initial fractionation on Sepharose CL-2B, the HTBM-containing fraction was subjected to reductive methylation and then gel filtration. Pure HTBM was employed in an overlay binding assay to identify the bacterial adhesin(s) and mucin receptors that participate in mucin-P. aeruginosa interactions. An approximately 16-kDa nonpilus protein component(s) of P. aeruginosa was found to be the adhesin(s) for HTBM. The mucin receptor for the 16-kDa component(s) was found in the peptide moiety. This study confirms that P. aeruginosa utilizes the nonpilus adhesin(s) to bind to HTBM. Identification of the specificity of the HTBM-P. aeruginosa interactions can lead to a better understanding of the predominance of P. aeruginosa colonization in individuals with cystic fibrosis.