Journal
BIOPHYSICAL JOURNAL
Volume 101, Issue 5, Pages 1257-1269Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2011.06.057
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Funding
- Foundation for Strategic Research and Vinnova (Sweden)
- Japan Science and Technology
- Swedish Research Council
- Swedish Cancer foundation
- Royal Swedish Academy of Sciences
- Lars Hierta's foundation
- Magnus Bergvall's foundation
- Grants-in-Aid for Scientific Research [19058001] Funding Source: KAKEN
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The activity of natural killer (NK) cells is regulated by a fine-tuned balance between activating and inhibitory receptors. Dual-color fluorescence cross-correlation spectroscopy (FCCS) was used to directly demonstrate a so-called cis-interaction between a member of the inhibitory NK cell receptor family Ly49 (Ly49A), and its ligand, the major histocompatibility complex (MHC) class I, within the plasma membrane of the same cell. By a refined FCCS model, calibrated by positive and negative control experiments on cells from the same lymphoid cell line, concentrations and diffusion coefficients of free and interacting proteins could be determined on a collection of cells. Using the intrinsic intercellular variation of their expression levels for titration, it was found that the fraction of Ly49A receptors bound in cis increase with increasing amounts of MHC class I ligand. This increase shows a tendency to be more abrupt than for a diffusion limited three dimensional bimolecular reaction, which most likely reflects the two-dimensional confinement of the reaction. For the Ly49A- MHC class I interaction it indicates that within a critical concentration range the local concentration level of MHC class I can provide a distinct regulation mechanism of the NK cell activity.
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