| Autor: |
Scharfman, Andree, Arora, Shiwani K., Delmotte, Philippe, Van Brussel, Edwige, Mazurier, Joel, Ramphal, Reuben, Roussel, Philippe |
| Zdroj: |
Infection and Immunity; September 2001, Vol. 69 Issue: 9 p5243-5248, 6p |
| Abstrakt: |
ABSTRACTPseudomonas aeruginosabinds to human respiratory mucins by mechanisms involving flagellar component-receptor interactions. The adhesion of P. aeruginosastrain PAK is mediated by the flagellar cap protein, FliD, without the involvement of flagellin. Two distinct types of FliD proteins have been identified inP. aeruginosa: A type, found in strain PAK, and B type, found in strain PAO1. In the present work, studies performed with theP. aeruginosaB-type strain PAO1 indicate that both the FliD protein and the flagellin of this strain are involved in the binding to respiratory mucins. Using polyacrylamide-based fluorescent glycoconjugates in a flow cytometry assay, it was previously demonstrated that P. aeruginosarecognizes Lex(or Lewis x) derivatives found at the periphery of human respiratory mucins. The aim of the present work was therefore to determine whether these carbohydrate epitopes (or glycotopes) are receptors for FliD proteins and flagellin. The results obtained by both flow cytometry and a microplate adhesion assay indicate that the FliD protein of strain PAO1 is involved in the binding of glycoconjugates bearing Lexor sialyl-Lexdeterminants, while the binding of flagellin is restricted to the glycoconjugate bearing Lexglycotope. In contrast, the type A cap protein ofP. aeruginosastrain PAK is not involved in the binding to glycoconjugates bearing Lex, sialyl-Lex, or sulfosialyl-Lexglycotopes. This study demonstrates a clear association between a specificPseudomonasadhesin and a specific mucin glycotope and demonstrates that fine specificities exist in mucin recognition by P. aeruginosa. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
