Influenza A M2 Channel Clustering at High Protein/Lipid Ratios: Viral Budding Implications

Biophysical Journal
Joana PaulinoTimothy A Cross

Abstract

Protein dynamics in crowded environments is important for understanding protein functions in vivo and is especially relevant for membrane proteins because of the roles of protein-protein interactions in membrane protein functions and their regulation. Here, using solid-state NMR spectroscopy in combination with coarse-grained molecular dynamics simulations, we report that the rotational correlation time for the transmembrane domain of the influenza A M2 proton channel in lipid bilayers increases dramatically at an elevated protein/lipid ratio. This increase is attributable to persistent protein-protein interactions, thus revealing for the first time, to the best of our knowledge, extensive cluster formation of the M2 tetrameric channel. Such clustering appears to have direct biological relevance during budding of the nascent influenza virus, which does not use the endosomal sorting complexes required for transport machinery. Indeed, initial coarse-grained molecular dynamics simulations of the longer M2 construct known as the conductance domain suggest clustering-induced membrane curvature formation.

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Citations

Feb 6, 2020·Proceedings of the National Academy of Sciences of the United States of America·Hedieh TorabifardCharles L Brooks
May 1, 2019·Proceedings of the National Academy of Sciences of the United States of America·Sören von BülowGerhard Hummer
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May 14, 2021·The Journal of Physical Chemistry. B·Yuqin YangHuan-Xiang Zhou
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
Jan 29, 2022·Journal of the American Chemical Society·Anna K WrightTimothy A Cross

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