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Protein engineering

Tighter ties that bind

Nature volume 484, pages 463–464 (2012)Cite this article

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A stepwise process of mutation and structural analysis has modulated a flexible binding interface of an immune-cell signalling protein, interleukin-2, and generated mutant proteins with enhanced anticancer activity. See Article p.529

Interleukin-2 is a cytokine protein that signals to cells of the immune system, such as T cells and natural killer cells, to regulate their growth, activation and differentiation. This multifaceted role means that interleukin-2 (IL-2) is the subject of intense investigation as a potential therapeutic agent to boost immune responses in the treatment of diseases such as cancer. On page 529 of this issue, Levin et al.1 describe the engineering of enhanced versions of IL-2 that more potently stimulate T-cell proliferation and antitumour immune responses. The authors also provide a compelling structural explanation for the mutated proteins' superior activity.

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Figure 1: Signalling superpowers.

References

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  1. Eric T. Boder is in the Department of Chemical and Biomolecular Engineering, University of Tennessee, Knoxville, Tennessee 37996-2200, USA.,

    Eric T. Boder

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  1. Eric T. Boder
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Correspondence to Eric T. Boder.

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Boder, E. Tighter ties that bind. Nature 484, 463–464 (2012). https://doi.org/10.1038/484463a

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