Pseudomonas aeruginosa exoenzyme S is an adhesion

Abstract

Exoenzyme S from Pseudomonas aeruginosa has been studied as an adhesin for glycosphingolipids and buccal cells. Binding of exoenzyme S to gangliotriosylceramide (GalNAcfll-4Gal,l-4Glci3l-1Cer), gangliotetraosylceramide (Gall-3GaINAcTIIl-4Gal1l-4Glcil-lCer), and lactosylceramide (Gal31-4Glco1-lCer) separated on thin-layer chromatograms was observed. Binding curves for exoenzyme S with dilutions of gangliotetraosylceramide immobilized on plastic plates were similar to previously reported results for the intact bacteria. Binding of exoenzyme S to sialylated counterparts of these glycosphingolipids was not seen, indicating that the addition of a sialic acid residue interferes with binding. Exoenzyme S and monoclonal antibody to exoenzyme S inhibit the binding of P. aeruginosa to buccal cells. The presence of exoenzyme S on the surface of P. aeruginosa was detected by immunogold labeling of bacteria with antibodies to exoenzyme S. Results of these studies led us to conclude that exoenzyme S is an important adhesin of P. aeruginosa. Pseudomonas aeruginosa is an important opportunistic pathogen of immunocompromised patients (7). Infections of the respiratory tract are of particular concern because they are associated with high mortality rates (2). Cystic fibrosis patients are at high risk for lung infections due to P. aeruginosa which lead to significant morbidity and contribute to death of the patients (15, 17). Identification of the factors responsible for colonization of the lungs of cystic fibrosis patients by P. aeruginosa is particularly important since the organism is virtually impossible to eradicate once a chronic infection has been established.

Genetic analysis of Pseudomonas aeruginosa adherence: distinct genetic loci control attachment to epithelial cells and mucins

“…8A). Furthermore, pilin antigen was not detected in the same bacteria (data not shown), confirming that the adhesive phenotype of these mutants was not due to restoration or hyperproduction of pili but, rather, was the consequence of Baker et al suggested that another bacterial product, exoenzyme S, functions as an adhesin (2). We have examined the nonadhering mutants, as well as adhesive rpoN variants, for expression of exoenzyme S. Figure 8B shows that all nonadhering mutants produced exoenzyme S at the level comparable to that in the wild-type parent.…”

“…Several P. aeruginosa virulence determinants have been implicated in mediating this phase of the bacterium-host interaction. These included pili (25,26), alginate (17), and, more recently, exoenzyme S (2). P. aeruginosa has been shown to recognize receptors on both epithelial cells and mucin.…”

The binding of Pseudomonas aeruginosa pili to glycosphingolipids is a tip‐associated event involving the C‐terminal region of the structural pilin subunit

“…The P, aeruginosa exoenzyme S functions as an adhesin that binds to giycosphingolipids (Baker et al, 1991;Lingwood et al, 1991). The occurrence of glycolipid receptors is commonly observed with Neisseria gonorrhoeae (Deal and Krivan.…”

Interaction between Aspergillus fumigatus and basement membrane laminin: Binding and substrate degradation

“…This strongly suggests that this enzyme, which can be active at physiological pH [24], plays an important role in basement membrane damages in vivo. It will be also interesting to determine if this enzyme is an adhesin as described for the exoenzyme S of P aeruginosa [5] and the fibrinogen binding and degrading components of Bacteroides gingivalis [23].…”