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Title: Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins

Abstract

Membranes proteins make up more than 60% of current drug targets and account for approximately 30% or more of the cellular proteome. Access to this important class of proteins has been difficult due to their inherent insolubility and tendency to aggregate in aqueous solutions. Understanding membrane protein structure and function demands novel means of membrane protein production that preserve both their native conformational state as well as function. Over the last decade, cell-free expression systems have emerged as an important complement to cell-based expression of membrane proteins due to their simple and customizable experimental parameters. One approach to overcome the solubility and stability limitations of purified membrane proteins is to support them in stable, native-like states within nanolipoprotein particles (NLPs), aka nanodiscs. This has become common practice to facilitate biochemical and biophysical characterization of proteins of interest. NLP technology can be easily coupled with cell-free systems to achieve functional membrane protein production for this purpose. Our approach involves utilizing cell-free expression systems in the presence of NLPs or using co-translation techniques to perform one-pot expression and self-assembly of membrane protein/NLP complexes. We describe how cell-free reactions can be modified to render control over nanoparticle size and monodispersity in support ofmore » membrane protein production. These modifications have been exploited to facilitate co-expression of full-length functional membrane proteins such as G-protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). In particular, we summarize the state of the art in NLP-assisted cell-free coexpression of these important classes of membrane proteins as well as evaluate the advances in and prospects for this technology that will drive drug discovery against these targets. We conclude with a prospective on the use of NLPs to produce as well as deliver functional mammalian membrane-bound proteins for a range of applications.« less

Authors:
; ; ; ;
Publication Date:
Research Org.:
Lawrence Livermore National Laboratory (LLNL), Livermore, CA (United States)
Sponsoring Org.:
USDOE National Nuclear Security Administration (NNSA)
OSTI Identifier:
1530895
Alternate Identifier(s):
OSTI ID: 1557951
Report Number(s):
LLNL-JRNL-768744
Journal ID: ISSN 1663-9812; 744
Grant/Contract Number:  
AC52-07NA27344
Resource Type:
Published Article
Journal Name:
Frontiers in Pharmacology
Additional Journal Information:
Journal Name: Frontiers in Pharmacology Journal Volume: 10; Journal ID: ISSN 1663-9812
Publisher:
Frontiers Media SA
Country of Publication:
Switzerland
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; cell-free; co-translation; nanolipoprotein particle; nanodisc; membrane proteins

Citation Formats

Shelby, Megan L., He, Wei, Dang, Amanda T., Kuhl, Tonya L., and Coleman, Matthew A.. Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins. Switzerland: N. p., 2019. Web. doi:10.3389/fphar.2019.00744.
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Shelby, Megan L., He, Wei, Dang, Amanda T., Kuhl, Tonya L., & Coleman, Matthew A.. Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins. Switzerland. https://doi.org/10.3389/fphar.2019.00744
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Shelby, Megan L., He, Wei, Dang, Amanda T., Kuhl, Tonya L., and Coleman, Matthew A.. Wed . "Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins". Switzerland. https://doi.org/10.3389/fphar.2019.00744.
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@article{osti_1530895,
title = {Cell-Free Co-Translational Approaches for Producing Mammalian Receptors: Expanding the Cell-Free Expression Toolbox Using Nanolipoproteins},
author = {Shelby, Megan L. and He, Wei and Dang, Amanda T. and Kuhl, Tonya L. and Coleman, Matthew A.},
abstractNote = {Membranes proteins make up more than 60% of current drug targets and account for approximately 30% or more of the cellular proteome. Access to this important class of proteins has been difficult due to their inherent insolubility and tendency to aggregate in aqueous solutions. Understanding membrane protein structure and function demands novel means of membrane protein production that preserve both their native conformational state as well as function. Over the last decade, cell-free expression systems have emerged as an important complement to cell-based expression of membrane proteins due to their simple and customizable experimental parameters. One approach to overcome the solubility and stability limitations of purified membrane proteins is to support them in stable, native-like states within nanolipoprotein particles (NLPs), aka nanodiscs. This has become common practice to facilitate biochemical and biophysical characterization of proteins of interest. NLP technology can be easily coupled with cell-free systems to achieve functional membrane protein production for this purpose. Our approach involves utilizing cell-free expression systems in the presence of NLPs or using co-translation techniques to perform one-pot expression and self-assembly of membrane protein/NLP complexes. We describe how cell-free reactions can be modified to render control over nanoparticle size and monodispersity in support of membrane protein production. These modifications have been exploited to facilitate co-expression of full-length functional membrane proteins such as G-protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). In particular, we summarize the state of the art in NLP-assisted cell-free coexpression of these important classes of membrane proteins as well as evaluate the advances in and prospects for this technology that will drive drug discovery against these targets. We conclude with a prospective on the use of NLPs to produce as well as deliver functional mammalian membrane-bound proteins for a range of applications.},
doi = {10.3389/fphar.2019.00744},
journal = {Frontiers in Pharmacology},
number = ,
volume = 10,
place = {Switzerland},
year = {2019},
month = {7}
}
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    Works referencing / citing this record:

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    Characterizing diffusion dynamics of a membrane protein associated with nanolipoproteins using fluorescence correlation spectroscopy
    journal, January 2011

    • Gao, Tingjuan; Blanchette, Craig D.; He, Wei
    • Protein Science, Vol. 20, Issue 2
    • DOI: 10.1002/pro.577

    Nanodisc-solubilized membrane protein library reflects the membrane proteome
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    • Marty, Michael T.; Wilcox, Kyle C.; Klein, William L.
    • Analytical and Bioanalytical Chemistry, Vol. 405, Issue 12
    • DOI: 10.1007/s00216-013-6790-8

    Biomimetic tethered lipid membranes designed for membrane-protein interaction studies
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    Establishment and characterization of cell-free translation/glycosylation in insect cell ( Spodoptera frugiperda 21) extract prepared with high pressure treatment
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    • DOI: 10.1016/j.ab.2010.11.021

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    α-Hemolysin pore formation into a supported phospholipid bilayer using cell-free expression
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    • Chalmeau, Jerome; Monina, Nadezda; Shin, Jonghyeon
    • Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. 1808, Issue 1
    • DOI: 10.1016/j.bbamem.2010.07.027

    Lipid–protein interactions in biological membranes: A dynamic perspective
    journal, February 2012

    Real-time monitoring of binding events on a thermostabilized human A2A receptor embedded in a lipid bilayer by surface plasmon resonance
    journal, May 2015

    • Bocquet, Nicolas; Kohler, Josiane; Hug, Melanie N.
    • Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. 1848, Issue 5
    • DOI: 10.1016/j.bbamem.2015.02.014

    Reconstitution of SNARE proteins into solid-supported lipid bilayer stacks and X-ray structure analysis
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    • Xu, Yihui; Kuhlmann, Jan; Brennich, Martha
    • Biochimica et Biophysica Acta (BBA) - Biomembranes, Vol. 1860, Issue 2
    • DOI: 10.1016/j.bbamem.2017.10.023

    Tethered bilayer lipid membranes (tBLMs): Interest and applications for biological membrane investigations
    journal, December 2014

    Kinetics of lipid mixing between bicelles and nanolipoprotein particles
    journal, February 2015

    Oriented Membrane Protein Reconstitution into Tethered Lipid Membranes for AFM Force Spectroscopy
    journal, November 2016

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    The role of HER2 in cancer therapy and targeted drug delivery
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    journal, June 2007

    • Klammt, Christian; Schwarz, Daniel; Eifler, Nora
    • Journal of Structural Biology, Vol. 158, Issue 3
    • DOI: 10.1016/j.jsb.2007.01.006

    Structural biology of G protein-coupled receptors: new opportunities from XFELs and cryoEM
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    Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins
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    Cell-free Co-expression of Functional Membrane Proteins and Apolipoprotein, Forming Soluble Nanolipoprotein Particles
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    Expression and Association of the Yersinia pestis Translocon Proteins, YopB and YopD, Are Facilitated by Nanolipoprotein Particles
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    Synthesis and biochemical characterization of EGF receptor in a water-soluble membrane model system
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    Challenges in the Development of Functional Assays of Membrane Proteins
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    Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs
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