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assessment of Pseudomonas aeruginosa lectin LecA binding characteristics of divalent galactosides using multiple techniques.
- Source :
- Glycobiology; Nov2021, Vol. 31 Issue 11, p1490-1499, 10p
- Publication Year :
- 2021
-
Abstract
- Pseudomonas aeruginosa is a widespread opportunistic pathogen that is capable of colonizing various human tissues and is resistant to many antibiotics. LecA is a galactose binding tetrameric lectin involved in adhesion, infection and biofilm formation. This study reports on the binding characteristics of mono- and divalent (chelating) ligands to LecA using different techniques. These techniques include affinity capillary electrophoresis, bio-layer interferometry, native mass spectrometry and a thermal shift assay. Aspects of focus include: affinity, selectivity, binding kinetics and residence time. The affinity of a divalent ligand was determined to be in the low-nanomolar range for all of the used techniques and with a ligand residence time of approximately 7 h, while no strong binding was seen to related lectin tetramers. Each of the used techniques provides a unique and complementary insight into the chelation based binding mode of the divalent ligand to the LecA tetramer. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09596658
- Volume :
- 31
- Issue :
- 11
- Database :
- Complementary Index
- Journal :
- Glycobiology
- Publication Type :
- Academic Journal
- Accession number :
- 154266271
- Full Text :
- https://doi.org/10.1093/glycob/cwab074