Comparison of lipidic carrier systems for integral membrane proteins - MsbA as case study

doi:10.1515/hsz-2019-0171

Comparative Study

. 2019 Oct 25;400(11):1509-1518.

doi: 10.1515/hsz-2019-0171.

Comparison of lipidic carrier systems for integral membrane proteins - MsbA as case study

Dominique-Maurice Kehlenbeck¹, Inokentijs Josts¹, Julius Nitsche¹, Sebastian Busch², V Trevor Forsyth^{3

4}, Henning Tidow¹

Affiliations

¹ The Hamburg Centre for Ultrafast Imaging and Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
² German Engineering Materials Science Centre (GEMS) at Heinz Maier-Leibnitz Zentrum (MLZ), Helmholtz-Zentrum Geesthacht, Lichtenbergstr. 1, 85747 Garching bei München, Germany.
³ Life Sciences Group, Institut Laue-Langevin, 6 Rue Jules Horowitz, 38042 Grenoble, France.
⁴ School of Life Sciences, Keele University, Staffordshire ST5 5BG, England.

PMID: 31141477
DOI: 10.1515/hsz-2019-0171

Comparative Study

Comparison of lipidic carrier systems for integral membrane proteins - MsbA as case study

Dominique-Maurice Kehlenbeck et al. Biol Chem. 2019.

. 2019 Oct 25;400(11):1509-1518.

doi: 10.1515/hsz-2019-0171.

Authors

Dominique-Maurice Kehlenbeck¹, Inokentijs Josts¹, Julius Nitsche¹, Sebastian Busch², V Trevor Forsyth^{3

4}, Henning Tidow¹

Affiliations

¹ The Hamburg Centre for Ultrafast Imaging and Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
² German Engineering Materials Science Centre (GEMS) at Heinz Maier-Leibnitz Zentrum (MLZ), Helmholtz-Zentrum Geesthacht, Lichtenbergstr. 1, 85747 Garching bei München, Germany.
³ Life Sciences Group, Institut Laue-Langevin, 6 Rue Jules Horowitz, 38042 Grenoble, France.
⁴ School of Life Sciences, Keele University, Staffordshire ST5 5BG, England.

PMID: 31141477
DOI: 10.1515/hsz-2019-0171

Abstract

Membrane protein research suffers from the drawback that detergents, which are commonly used to solubilize integral membrane proteins (IMPs), often lead to protein instability and reduced activity. Recently, lipid nanodiscs (NDs) and saposin-lipoprotein particles (Salipro) have emerged as alternative carrier systems that keep membrane proteins in a native-like lipidic solution environment and are suitable for biophysical and structural studies. Here, we systematically compare nanodiscs and Salipros with respect to long-term stability as well as activity and stability of the incorporated membrane protein using the ABC transporter MsbA as model system. Our results show that both systems are suitable for activity measurements as well as structural studies in solution. Based on our results we suggest screening of different lipids with respect to activity and stability of the incorporated IMP before performing structural studies.

Keywords: MsbA; Salipro; integral membrane proteins; nanodiscs; saposin-lipoprotein particles.

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References

1. Arana, M.R., Fiori, M.C., and Altenberg, G.A. (2019). Functional and structural comparison of the ABC exporter MsbA studied in detergent and reconstituted in nanodiscs. Biochem. Biophys. Res. Commun. 512, 448–452.
1. Autzen, H.E., Myasnikov, A.G., Campbell, M.G., Asarnow, D., Julius, D., and Cheng, Y. (2018). Structure of the human TRPM4 ion channel in a lipid nanodisc. Science 359, 228–232.
1. Baginski, E.S., Epstein, E., and Zak, B. (1975). Review of phosphate methodologies. Ann. Clin. Lab. Sci. 5, 399–416.
1. Barniol-Xicota, M. and Verhelst, S.H.L. (2018). Stable and functional rhomboid proteases in lipid nanodiscs by using diisobutylene/maleic acid copolymers. J. Am. Chem. Soc. 140, 14557–14561.
1. Bayburt, T.H. and Sligar, S.G. (2010). Membrane protein assembly into Nanodiscs. FEBS Lett. 584, 1721–1727.

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[1] Arana, M.R., Fiori, M.C., and Altenberg, G.A. (2019). Functional and structural comparison of the ABC exporter MsbA studied in detergent and reconstituted in nanodiscs. Biochem. Biophys. Res. Commun. 512, 448–452.

[2] Arana, M.R., Fiori, M.C., and Altenberg, G.A. (2019). Functional and structural comparison of the ABC exporter MsbA studied in detergent and reconstituted in nanodiscs. Biochem. Biophys. Res. Commun. 512, 448–452.

[3] Autzen, H.E., Myasnikov, A.G., Campbell, M.G., Asarnow, D., Julius, D., and Cheng, Y. (2018). Structure of the human TRPM4 ion channel in a lipid nanodisc. Science 359, 228–232.

[4] Autzen, H.E., Myasnikov, A.G., Campbell, M.G., Asarnow, D., Julius, D., and Cheng, Y. (2018). Structure of the human TRPM4 ion channel in a lipid nanodisc. Science 359, 228–232.

[5] Baginski, E.S., Epstein, E., and Zak, B. (1975). Review of phosphate methodologies. Ann. Clin. Lab. Sci. 5, 399–416.

[6] Baginski, E.S., Epstein, E., and Zak, B. (1975). Review of phosphate methodologies. Ann. Clin. Lab. Sci. 5, 399–416.

[7] Barniol-Xicota, M. and Verhelst, S.H.L. (2018). Stable and functional rhomboid proteases in lipid nanodiscs by using diisobutylene/maleic acid copolymers. J. Am. Chem. Soc. 140, 14557–14561.

[8] Barniol-Xicota, M. and Verhelst, S.H.L. (2018). Stable and functional rhomboid proteases in lipid nanodiscs by using diisobutylene/maleic acid copolymers. J. Am. Chem. Soc. 140, 14557–14561.

[9] Bayburt, T.H. and Sligar, S.G. (2010). Membrane protein assembly into Nanodiscs. FEBS Lett. 584, 1721–1727.

[10] Bayburt, T.H. and Sligar, S.G. (2010). Membrane protein assembly into Nanodiscs. FEBS Lett. 584, 1721–1727.

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Comparison of lipidic carrier systems for integral membrane proteins - MsbA as case study

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Comparison of lipidic carrier systems for integral membrane proteins - MsbA as case study

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