Structure binding relationship of galactosylated Glycoclusters toward Pseudomonas aeruginosa lectin LecA using a DNA-based carbohydrate microarray.

Pseudomonas aeruginosa (PA) is a major public health issue due to its impact on nosocomial infections as well as its impact on cystic fibrosis patient mortality. One of the main concerns is its ability to develop antibiotic resistance. Therefore, inhibition of PA virulence has been proposed as an alternative strategy to tackle PA based infections.

Synthesis of homo- and heterofunctionalized glycoclusters and binding to Pseudomonas aeruginosa lectins PA-IL and PA-IIL.

Homo- and heterofunctionalized glycoclusters with galactose and/or fucose residues targeting both PA-IL and PA-IIL lectins of Pseudomonas aeruginosa were synthesized using "Click" chemistry and DNA chemistry. Their binding to lectins (separately or in a mixture) was studied using a DNA Directed Immobilization carbohydrate microarray. Homoglycoclusters bind selectively to their lectin while the heteroglycocluster binds simultaneously both lectins with a slight lower affinity.

Quantitative analysis (K(d) and IC(50)) of glycoconjugates interactions with a bacterial lectin on a carbohydrate microarray with DNA Direct Immobilization (DDI).

Nowadays, there is a great interest for understanding the structure/function relationship governing recognition of carbohydrates by their receptors for the design of new treatments. Indeed, carbohydrates and glycoconjugates play a major role in key biological events such as cell-cell recognition, pathogenesis inflammation, and host pathogen interactions. Pseudomonas aeruginosa (PA) is one of the predominant bacterium encountered in nosocomial infections.

Synthesis of a library of fucosylated glycoclusters and determination of their binding toward Pseudomonas aeruginosa lectin B (PA-IIL) using a DNA-based carbohydrate microarray.

Pseudomonas aeruginosa (PA) is a Gram negative opportunistic pathogen and is the major pathogen encounter in the cystic fibrosis (CF) lung airways. It often leads to chronic respiratory infection despite aggressive antibiotic therapy due to the emergence of resistant strains and to the formation of biofilm. The lectin PA-IIL (LecB) is a fucose-specific lectin from PA suspected to be involved in host recognition/adhesion and in biofilm formation.

Multiplexed binding determination of seven glycoconjugates for Pseudomonas aeruginosa lectin I (PA-IL) using a DNA-based carbohydrate microarray.

The binding of seven multivalent glycoconjugates displaying linear or antenna-like structures and different electronic environments were evaluated towards PA-IL on a DNA-based carbohydrate microarray. The affinity can be modulated by the charge and the topology of the galactosylated derivatives.

Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.

Influenza neuraminidases hydrolyze the ketosidic linkage between N-acetylneuraminic acid and its adjacent galactose residue in sialosides. This enzyme is a tetrameric protein that plays a critical role in the release of progeny virions. Several methods have been described for the determination of neuraminidase activity, usually based on colorimetric, fluorescent, or chemiluminescent detection.