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Bacterial Surface Glycans: Microarray and QCM Strategies for Glycophenotyping and Exploration of Recognition by Host Receptors.
- Source :
-
Methods in enzymology [Methods Enzymol] 2018; Vol. 598, pp. 37-70. Date of Electronic Publication: 2017 Aug 10. - Publication Year :
- 2018
-
Abstract
- Bacterial surfaces are decorated with a diversity of carbohydrate structures that play important roles in the bacteria-host relationships. They may offer protection against host defense mechanisms, elicit strong antigenic responses, or serve as ligands for host receptors, including lectins of the innate immune system. Binding by these lectins may trigger defense responses or, alternatively, promote attachment, thereby enhancing infection. The outcome will depend on the particular bacterial surface landscape, which may substantially differ among species and strains. In this chapter, we describe two novel methods for exploring interactions directly on the bacterial surface, based on the generation of bacterial microarrays and quartz crystal microbalance (QCM) sensor chips. Bacterial microarrays enable profiling of accessible carbohydrate structures and screening of their recognition by host receptors, also providing information on binding avidity, while the QCM approach allows determination of binding affinity and kinetics. In both cases, the chief element is the use of entire bacterial cells, so that recognition of the bacterial glycan epitopes is explored in their natural environment.<br /> (© 2018 Elsevier Inc. All rights reserved.)
- Subjects :
- Host Microbial Interactions immunology
Kinetics
Klebsiella pneumoniae chemistry
Klebsiella pneumoniae immunology
Lectins chemistry
Ligands
Microarray Analysis instrumentation
Polysaccharides, Bacterial chemistry
Quartz Crystal Microbalance Techniques instrumentation
Receptors, Immunologic chemistry
Lectins immunology
Microarray Analysis methods
Polysaccharides, Bacterial immunology
Quartz Crystal Microbalance Techniques methods
Receptors, Immunologic immunology
Subjects
Details
- Language :
- English
- ISSN :
- 1557-7988
- Volume :
- 598
- Database :
- MEDLINE
- Journal :
- Methods in enzymology
- Publication Type :
- Academic Journal
- Accession number :
- 29306443
- Full Text :
- https://doi.org/10.1016/bs.mie.2017.06.011