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Making water-soluble integral membrane proteins in vivo using an amphipathic protein fusion strategy

Author

Listed:
  • Dario Mizrachi

    (School of Chemical and Biomolecular Engineering, Cornell University)

  • Yujie Chen

    (School of Applied and Engineering Physics, Cornell University)

  • Jiayan Liu

    (University of Michigan)

  • Hwei-Ming Peng

    (University of Michigan)

  • Ailong Ke

    (Cornell University)

  • Lois Pollack

    (School of Applied and Engineering Physics, Cornell University)

  • Raymond J. Turner

    (University of Calgary)

  • Richard J. Auchus

    (University of Michigan)

  • Matthew P. DeLisa

    (School of Chemical and Biomolecular Engineering, Cornell University)

Abstract

Integral membrane proteins (IMPs) play crucial roles in all cells and represent attractive pharmacological targets. However, functional and structural studies of IMPs are hindered by their hydrophobic nature and the fact that they are generally unstable following extraction from their native membrane environment using detergents. Here we devise a general strategy for in vivo solubilization of IMPs in structurally relevant conformations without the need for detergents or mutations to the IMP itself, as an alternative to extraction and in vitro solubilization. This technique, called SIMPLEx (solubilization of IMPs with high levels of expression), allows the direct expression of soluble products in living cells by simply fusing an IMP target with truncated apolipoprotein A-I, which serves as an amphipathic proteic ‘shield’ that sequesters the IMP from water and promotes its solubilization.

Suggested Citation

  • Dario Mizrachi & Yujie Chen & Jiayan Liu & Hwei-Ming Peng & Ailong Ke & Lois Pollack & Raymond J. Turner & Richard J. Auchus & Matthew P. DeLisa, 2015. "Making water-soluble integral membrane proteins in vivo using an amphipathic protein fusion strategy," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7826
    DOI: 10.1038/ncomms7826
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    Cited by:

    1. Kevin B. Weyant & Ayomide Oloyede & Sukumar Pal & Julie Liao & Mariela Rivera-De Jesus & Thapakorn Jaroentomeechai & Tyler D. Moeller & Steven Hoang-Phou & Sean F. Gilmore & Riya Singh & Daniel C. Pan, 2023. "A modular vaccine platform enabled by decoration of bacterial outer membrane vesicles with biotinylated antigens," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Mengke Li & Hongzhi Tang & Rui Qing & Yanze Wang & Jiongqin Liu & Rui Wang & Shan Lyu & Lina Ma & Ping Xu & Shuguang Zhang & Fei Tao, 2024. "Design of a water-soluble transmembrane receptor kinase with intact molecular function by QTY code," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    3. Qian Kang & Huan Fang & Mengjie Xiang & Kaixing Xiao & Pingtao Jiang & Chun You & Sang Yup Lee & Dawei Zhang, 2023. "A synthetic cell-free 36-enzyme reaction system for vitamin B12 production," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    4. Thapakorn Jaroentomeechai & Yong Hyun Kwon & Yiwen Liu & Olivia Young & Ruchika Bhawal & Joshua D. Wilson & Mingji Li & Digantkumar G. Chapla & Kelley W. Moremen & Michael C. Jewett & Dario Mizrachi &, 2022. "A universal glycoenzyme biosynthesis pipeline that enables efficient cell-free remodeling of glycans," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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