Kinetic and Structural Studies of Interactions between Glycosaminoglycans and Langerin

Jing Zhao, Xinyue Liu, Chelsea Kao, Emily Zhang, Quanhong Li, Fuming Zhang, Robert J. Linhardt

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

Langerin, a C-type lectin, is expressed in Langerhans cells. It was reported that langerin binds sulfated glycans, which is an important initial step for its role in blocking human immunodeficiency virus (HIV) transmission by capturing HIV pathogens and mediating their internalization into Birbeck granules for their elimination. It is fundamentally important to understand these interactions at the molecular level for the design of new highly specific therapeutic agents for HIV. Surface plasmon resonance (SPR), which allows for the real-time, direct, quantitative analysis of the label-free molecular interactions, has been used successfully for biophysical characterization of glycosaminoglycan (GAG)-protein interactions. In this study, we report kinetics, structural analysis, and the effects of physiological conditions (e.g., pH, salt concentration, and Ca2+ and Zn2+concentrations) on the interactions between GAGs and langerin using SPR. SPR results revealed that langerin binds to heparin with high affinity (KD ∼ 2.4 nM) and the oligosaccharide length required for the interactions is larger than a tetrasaccharide. This heparin/heparan sulfate-binding protein also interacts with other GAGs, including dermatan sulfate, chondroitin sulfates C-E and KS. In addition, liquid chromatography-mass spectrometry analysis was used to characterize the structure of sulfated glycans that bound to langerin.

Original languageEnglish
Pages (from-to)4552-4559
Number of pages8
JournalBiochemistry
Volume55
Issue number32
DOIs
StatePublished - 16 Aug 2016
Externally publishedYes

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