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Novel fluorescence assay for tracking molecular and cellular allegen-protein interaction.

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Thierse,  Hermann-Josef
Research Group and Chair of Molecular Immunology of the University of Freiburg, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Pink,  Matthias
Emeritus Group: Cellular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Weltzien,  Hans-Ulrich
Emeritus Group: Cellular Immunology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society;

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Citation

Thierse, H.-J., Helm, S., Pink, M., & Weltzien, H.-U. (2007). Novel fluorescence assay for tracking molecular and cellular allegen-protein interaction. Journal of Immunological Methods, 328, 14-20.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-91FC-B
Abstract
T cells recognizing nickel (Ni) are key mediators in human Ni allergy, which represents the most common form of human contact hypersensitivity. In contrast to well-characterized Ni-specific human T cell clones, molecular knowledge about the extra- and intracellular route(s) of antigen/allergen presentation and processing of Ni-specific epitopes is still fragmentary. Here, we demonstrate a new metal-specific fluorescent technique to detect and quantify metal ions, like Ni2+, while they are associated with isolated metalloproteins. Moreover, utilizing the fluorescent metal sensor molecule Newport Green (NPG) a novel method has been developed, which permits the metal-specific detection of Ni2+ binding to surface or intracellular structures of individual human antigen presenting cells by flow cytometry. We expect such metal-specific fluorescent analyses to contribute to a better basic understanding of molecular and cellular immune processes involved in Ni-specific T cell epitope generation and the pathogenesis of human nickel allergy.