title: Recognition of Lewis x derivatives present on mucins by flagellar components of Pseudomonas aeruginosa.
abstract: Pseudomonas aeruginosa binds to human respiratory mucins by mechanisms involving flagellar component-receptor interactions. The adhesion of P. aeruginosa strain PAK is mediated by the flagellar cap protein, FliD, without the involvement of flagellin. Two distinct types of FliD proteins have been identified in P. aeruginosa: A type, found in strain PAK, and B type, found in strain PAO1. In the present work, studies performed with the P. aeruginosa B-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. aeruginosa recognizes Le(x) (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 Le(x) or sialyl-Le(x) determinants, while the binding of flagellin is restricted to the glycoconjugate bearing Le(x) glycotope. In contrast, the type A cap protein of P. aeruginosa strain PAK is not involved in the binding to glycoconjugates bearing Le(x), sialyl-Le(x), or sulfosialyl-Le(x) glycotopes. This study demonstrates a clear association between a specific Pseudomonas adhesin and a specific mucin glycotope and demonstrates that fine specificities exist in mucin recognition by P. aeruginosa.
authors.affiliation: Unité INSERM No. 377 and Université de Lille 2, 59045 Lille Cedex, France.
authors.forename: A
authors.initials: A
authors.lastname: Scharfman
authors.forename: S K
authors.initials: SK
authors.lastname: Arora
authors.forename: P
authors.initials: P
authors.lastname: Delmotte
authors.forename: E
authors.initials: E
authors.lastname: Van Brussel
authors.forename: J
authors.initials: J
authors.lastname: Mazurier
authors.forename: R
authors.initials: R
authors.lastname: Ramphal
authors.forename: P
authors.initials: P
authors.lastname: Roussel
mesh_terms: D001422:Bacterial Adhesion; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D005408:Flagellin / Q000235:genetics / Q000378:metabolism; D005434:Flow Cytometry; D006001:Glycoconjugates / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D016256:Lewis X Antigen / Q000737:chemistry / Q000378:metabolism*; D009077:Mucins / Q000737:chemistry* / Q000378:metabolism*; D009154:Mutation; D009844:Oligosaccharides / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D011550:Pseudomonas aeruginosa / Q000502:physiology*; D020545:Respiratory Mucosa / Q000378:metabolism; D000080506:Sialyl Lewis X Antigen / Q000031:analogs & derivatives
chemical_list: C086949:6'-sulfated sialyl Lewis x; D001426:Bacterial Proteins; D006001:Glycoconjugates; D016256:Lewis X Antigen; D009077:Mucins; D009844:Oligosaccharides; D000080506:Sialyl Lewis X Antigen; D005408:Flagellin; C076733:FlaD protein, Bacteria