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Fluorescent labeling agents change binding profiles of glycan-binding proteins

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Molecular BioSystems Vol - 7 Issue - 9

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Fluorescent labeling agents change binding profiles of glycan-binding proteins

Content Provider	Royal Society of Chemistry (RSC)
Author	Sun, Yung-Shin Chen, Xi Landry, James P. Chokhawala, Harshal A. Huang, Shengshu Li, Yanhong Lau, Kam Zhu, Xiangdong Fei, Yiyan Yu, Hai
Copyright Year	2011
Abstract	Interactions of glycan-binding proteins (GBPs) with glycans are essential in cell adhesion, bacterial/viral infection, and cellular signaling pathways. Experimental characterization of these interactions based on glycan microarrays typically involves (1) labeling GBPs directly with fluorescent reagents before incubation with the microarrays, or (2) labeling GBPs with biotin before the incubation and detecting the captured GBPs after the incubation using fluorescently labeled streptavidin, or (3) detecting the captured GBPs after the incubation using fluorescently labeled antibodies raised against the GBPs. The fluorescent signal is mostly measured ex situ after excess fluorescent materials are washed off. In this study, by using a label-free optical scanner for glycan microarray detection, we measured binding curves of 7 plant lectins to 24 glycans: four β1-4-linked galactosides, three β1-3-linked galactosides, one β-linked galactoside, one α-linked N-acetylgalactosaminide, eight α2-3-linked sialosides, and seven α2-6-linked sialosides. From association and dissociation constants deduced by global-fitting the binding curves, we found that (1) labeling lectins directly with fluorescent agents change binding profiles of lectins, in some cases by orders of magnitude; (2) those lectin–glycan binding reactions characterized with large dissociation rates, though biologically relevant, are easily missed or deemed insignificant in ex situ fluorescence-based assays as most captured lectins are washed off before detection. This study highlights the importance of label-free real-time detection of protein–ligand interactions and the potential pitfall in interpreting fluorescence-based assays for characterization of protein–glycan interactions.
Starting Page	3343
Ending Page	3352
Page Count	10
File Format	HTM / HTML PDF
ISSN	1742206X
Volume Number	7
Issue Number	12
Journal	Molecular BioSystems
DOI	10.1039/c1mb05332a
Language	English
Publisher	Royal Society of Chemistry
Access Restriction	Open
Subject Keyword	Antibody Cell adhesion Streptavidin Galactoside Biotin Dissociative Microarray Glycan
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Biotechnology

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Fluorescent Labeling Agents Change Binding Profiles of Glycan-Binding Proteins

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Fluorescent labeling agents change binding profiles of glycan-binding proteins

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