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Total chemical synthesis of an Orf virus protein, ORFV002, an inhibitor of the master gene regulator NF-κB

Authors

  • S. J. Son,

    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
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  • P. W. R. Harris,

    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
    2. School of Chemical Sciences, The University of Auckland, Auckland, New Zealand
    3. Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand
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  • C. J. Squire,

    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
    2. Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand
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  • E. N. Baker,

    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
    2. Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand
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  • S. B. H. Kent,

    1. Department of Chemistry, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL, United States
    2. Department of Biochemistry and Molecular Biology, Institute for Biophysical Dynamics, University of Chicago, Chicago, IL, United States
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  • M. A. Brimble

    Corresponding author
    1. School of Biological Sciences, The University of Auckland, Auckland, New Zealand
    2. School of Chemical Sciences, The University of Auckland, Auckland, New Zealand
    3. Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand
    • Correspondence to: M. A. Brimble, School of Biological Sciences, The University of Auckland, Private Bag 92019, Auckland 1142, New Zealand; e-mail: m.brimble@auckland.ac.nz

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  • This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com

ABSTRACT

ORFV002 is a novel orf viral protein (117 Aa) that inhibits nuclear events through the regulation of the transcriptional activity of NF-κB, a master regulator of human gene expression (Diel et al., J Virol 2011, 85, 264–275). It is identified as the first nuclear inhibitor of NF-κB produced by orf virus (ORFV) and no homologues in other genera of the Chordopoxvirinae subfamily have been reported to date (Diel et al., J Virol 2011, 85, 264–275). Our molecular structure predictions suggest that ORFV002 may mimic part of IκB, an inhibitor and natural human partner of NF-κB. Recent advances in total chemical synthesis of proteins have provided solutions in overcoming challenges of current recombinant methods of protein isolation for structure elucidation. Aided by Boc solid phase peptide synthesis and native chemical ligation, ORFV002 was successfully synthesized in multimilligram amounts in good yield and high purity. © 2013 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 137–144, 2014.

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