Investigation of the curvature induction and membrane localization of the influenza virus M2 protein using static and off-magic-angle spinning solid-state nuclear magnetic resonance of oriented bicelles

Biochemistry
Tuo Wang, Mei Hong

Abstract

A wide variety of membrane proteins induce membrane curvature for function; thus, it is important to develop new methods to simultaneously determine membrane curvature and protein binding sites in membranes with multiple curvatures. We introduce solid-state nuclear magnetic resonance (NMR) methods based on magnetically oriented bicelles and off-magic-angle spinning (OMAS) to measure membrane curvature and the binding site of proteins in mixed-curvature membranes. We demonstrate these methods on the influenza virus M2 protein, which not only acts as a proton channel but also mediates virus assembly and membrane scission. An M2 peptide encompassing the transmembrane (TM) domain and an amphipathic helix, M2(21-61), was studied and compared with the TM peptide (M2TM). Static (31)P NMR spectra of magnetically oriented 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC)/1,2-dihexanoyl-sn-glycero-3-phosphocholine (DHPC) bicelles exhibit a temperature-independent isotropic chemical shift in the presence of M2(21-61) but not M2TM, indicating that the amphipathic helix confers the ability to generate a high-curvature phase. Two-dimensional (2D) (31)P spectra indicate that this high-curvature phase is associated with the DHPC bicelle edges...Continue Reading

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Citations

Nov 26, 2015·Progress in Nuclear Magnetic Resonance Spectroscopy·Rachel W MartinKelsey A Collier
Jun 11, 2016·Langmuir : the ACS Journal of Surfaces and Colloids·Chian Sing HoJianjun Pan
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Jul 10, 2020·The Journal of Physical Chemistry. B·Agnieszka MartynaJeremy S Rossman
Oct 30, 2021·Journal of Chemical Information and Modeling·Dimitrios KolokourisAntonios Kolocouris

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