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Thermostable tag (TST) protein expression system: Engineering thermotolerant recombinant proteins and vaccines

  1. Author:
    Luke, J. M.
    Carnes, A. E.
    Sun, P.
    Hodgson, C. P.
    Waugh, D. S.
    Williams, J. A.
  2. Author Address

    [Williams, James A.] Nat Technol Corp, Res & Dev, Lincoln, NE 68521 USA. [Sun, Ping; Waugh, David S.] NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA.;Williams, JA, Nat Technol Corp, Res & Dev, 4701 Innovat Dr, Lincoln, NE 68521 USA.;jim@natx.com
    1. Year: 2011
    2. Date: Feb
  1. Journal: Journal of Biotechnology
    1. 151
    2. 3
    3. Pages: 242-250
  2. Type of Article: Article
  3. ISSN: 0168-1656
  1. Abstract:

    Methods to increase temperature stability of vaccines and adjuvants are needed to reduce dependence on cold chain storage. We report herein creation and application of pVEX expression vectors to improve vaccine and adjuvant manufacture and thermostability. Defined media fermentation yields of 6 g/L thermostable toll-like receptor 5 agonist flagellin were obtained using an IPTG inducible pVEX-flagellin expression vector. Alternative pVEX vectors encoding Pyrococcus furiosus maltodextrin-binding protein (pfMBP) as a fusion partner improved Influenza hemagglutinin antigen vaccine solubility and thermostability. A pfMBP hemagglutinin HA2 domain fusion protein was a potent immunogen. Manufacturing processes that combined up to 5 g/L defined media fermentation yields with rapid, selective, thermostable pfMBP fusion protein purification were developed. The pVEX pfMBP-based thermostable tag (TST) platform is a generic protein engineering approach to enable high yield manufacture of thermostable recombinant protein vaccine components. (C) 2010 Elsevier B.V. All rights reserved.

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External Sources

  1. DOI: 10.1016/j.jbiotec.2010.12.011
  2. WOS: 000287427600002

Library Notes

  1. Fiscal Year: FY2010-2011
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