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Self-reporting peptides illuminate the MHC groove

Nature Chemical Biology volume 3, pages 201–202 (2007)Cite this article

Synthetic oligopeptides chemically modified with environmentally sensitive fluorophores enable real-time visualization of peptide binding to MHC molecules. This technology will expand our understanding of antigen presentation and enable visualization of fluorescent peptide binding to a wide variety of receptors in living cells.

Major histocompatibility complex (MHC) molecules present oligopeptides peptide antigens from immunogenic proteins to activate T-cell responses. A critical aspect of antigen presentation is peptide binding to MHC molecules. Only ∼1% of peptides of sufficient length are able to bind to any given MHC class I or class II gene product. Though numerous methods exist for quantitating peptide binding to MHC molecules, none detects binding in real time—until now, that is. In this issue of Nature Chemical Biology, Venkatraman et al.1 report that upon binding to the human MHC class II molecule DR1, peptides modified with environmentally sensitive fluorophores demonstrate large increases in fluorescence, an increased Stokes shift in emission, and increased fluorescence lifetime, all of which can be exploited to monitor peptide binding in real time.

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Figure 1: Location, location, location: self-reporting peptides identify peptide-receptive MHC molecules.

Katie Ris

References

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  1. Jonathan W. Yewdell and Avital Lev are in the Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Building 33, 33 North Drive, US National Institutes of Health, Bethesda, Maryland 20892, USA. jyewdell@nih.gov,

    Jonathan W Yewdell & Avital Lev

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  1. Jonathan W Yewdell
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  2. Avital Lev
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Yewdell, J., Lev, A. Self-reporting peptides illuminate the MHC groove. Nat Chem Biol 3, 201–202 (2007). https://doi.org/10.1038/nchembio0407-201

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  • DOI: https://doi.org/10.1038/nchembio0407-201

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