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In vivo post-translational modifications of recombinant mussel adhesive protein in insect cells

Authors

  • Seonghye Lim,

    1. Dept. of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea
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  • Kyoung Ro Kim,

    1. Dept. of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea
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    • Seonghye Lim and Kyoung Ro Kim contributed equally to this work.

  • Yoo Seong Choi,

    1. Dept. of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea
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  • Dae-Kyum Kim,

    1. Dept. of Life Science, Pohang University of Science and Technology, Pohang 790-784, Korea
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  • Daehee Hwang,

    1. Dept. of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea
    2. School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang 790-784, Korea
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  • Hyung Joon Cha

    Corresponding author
    1. Dept. of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea
    2. Ocean Science and Technology Institute, Pohang University of Science and Technology, Pohang 790-784, Korea
    • Dept. of Chemical Engineering, Pohang University of Science and Technology, Pohang 790-784, Korea
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Abstract

Mussel adhesive proteins (MAPs) have been suggested as promising bioadhesives for diverse application fields, including medical uses. Previously, we successfully constructed and produced a new type of functional recombinant MAP, fp-151, in a prokaryotic Escherichia coli expression system. Even though the E. coli-derived MAP showed several excellent features, such as high production yield and efficient purification, in vitro enzymatic modification is required to convert tyrosine residues to l-3,4-dihydroxyphenyl alanine (dopa) molecules for its adhesive ability, due to the intrinsic inability of E. coli to undergo post-translational modification. In this work, we produced a soluble recombinant MAP in insect Sf9 cells, which are widely used as an effective and convenient eukaryotic expression system for eukaryotic foreign proteins. Importantly, we found that insect-derived MAP contained converted dopa residues by in vivo post-translational modification. In addition, insect-derived MAP also had other post-translational modifications including phosphorylation of serine and hydroxylation of proline that originally occurred in some natural MAPs. To our knowledge, this is the first report on in vivo post-translational modifications of MAP containing dopa and other modified amino acid residues. © 2011 American Institute of Chemical Engineers Biotechnol. Prog., 2011

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