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Next-generation protein engineering targets influenza

Nature Biotechnology volume 30, pages 502–504 (2012)Cite this article

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Computational design and high-throughput mutational scanning yield proteins with subnanomolar affinities for influenza hemagglutinin.

The development of engineering principles for the design of protein-protein interactions requires a deep understanding of the protein-association process. A major impediment to progress has been the lack of large data sets—on structures of protein complexes, on binding affinities and on the functional effects of mutations. High-throughput DNA sequencing enables parallel acquisition of gigabases of sequence data at low cost and has transformed many areas in biology beyond genome sequencing. Applied in conjunction with in vitro selection, it is becoming the method of choice for experimentally determining the landscapes of sequence-function relationships in a range of systems, including antibody-antigen4, protein-peptide5,6 and protein-DNA7 interactions.

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Figure 1: Use of next-generation sequencing to identify variants of designed proteins HB80.3 and HB36.4 that bind H1N1 influenza hemagglutinin with high affinity.

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Authors and Affiliations

  1. and the Departments of Molecular Genetics and Biochemistry, Shoshana J. Wodak is in the Molecular Structure and Function Program, Hospital for Sick Children, Toronto, Ontario, Canada, University of Toronto, Toronto, Ontario, Canada.,

    Shoshana J Wodak

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  1. Shoshana J Wodak
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Correspondence to Shoshana J Wodak.

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The author declares no competing financial interests.

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Wodak, S. Next-generation protein engineering targets influenza. Nat Biotechnol 30, 502–504 (2012). https://doi.org/10.1038/nbt.2268

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