16 research outputs found
Multivalent glycoconjugates as anti-pathogenic agents
Multivalency plays a major role in biological processes and particularly in the relationship between pathogenic microorganisms and their host
that involves protein–glycan recognition. These interactions occur during the first steps of infection, for specific recognition between host and
bacteria, but also at different stages of the immune response. The search for high-affinity ligands for studying such interactions involves the
combination of carbohydrate head groups with different scaffolds and linkers generating multivalent glycocompounds with controlled spatial
and topology parameters. By interfering with pathogen adhesion, such glycocompounds including glycopolymers, glycoclusters,
glycodendrimers and glyconanoparticles have the potential to improve or replace antibiotic treatments that are now subverted by resistance.
Multivalent glycoconjugates have also been used for stimulating the innate and adaptive immune systems, for example with carbohydrate-based
vaccines. Bacteria present on their surfaces natural multivalent glycoconjugates such as lipopolysaccharides and S-layers that can also be
exploited or targeted in anti-infectious strategie
Special Issue dedicated to Karl-Erich Jaeger on the occasion of his 60th birthday
This issue of the Journal of Biotechnology is dedicated to our mentor, colleague and dear friend Karl-Erich Jaeger (KEJ). Thus, it is our great pleasure to honor KEJ on the occasion of his 60th birthday
Specific Association of Lectin LecB with the Surface of Pseudomonas aeruginosa: Role of Outer Membrane Protein OprF
The fucose binding lectin LecB affects biofilm formation and is involved in pathogenicity of Pseudomonas aeruginosa. LecB resides in the outer membrane and can be released specifically by treatment of an outer membrane fraction with fucose suggesting that it binds to specific ligands. Here, we report that LecB binds to the outer membrane protein OprF. In an OprF-deficient P. aeruginosa mutant, LecB is no longer detectable in the membrane but instead in the culture supernatant indicating a specific interaction between LecB and OprF