期刊
BIOCHEMISTRY
卷 55, 期 32, 页码 4552-4559出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.biochem.6b00555
关键词
-
资金
- National Institutes of Health [HL062244, HL094463]
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 similar to 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.
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