Bernardi, A, Jiménez-Barbero, J, Casnati, A et al. (30 more authors) (2013) Multivalent glycoconjugates as anti-pathogenic agents. Chemical Society Reviews, 42 (11). 4709 - 4727. ISSN 0306-0012
Abstract
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 strategies.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | (c) 2013, The Royal Society of Chemists. This is an open access article under the terms of the Creative Commons Attribution License CC-BY. |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 16 Jul 2014 14:49 |
Last Modified: | 17 Jan 2018 03:41 |
Published Version: | http://dx.doi.org/10.1039/c2cs35408j |
Status: | Published |
Publisher: | Royal Society of Chemistry |
Identification Number: | 10.1039/c2cs35408j |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:79773 |