The M2 protein of the Influenza A virus mediates the acidification of the viron interior at low pH conditions, a step vital to viral replication. High-resolution structural studies reveal that the transmebrane (TM) portion of the M2 protein is composed of four identical helices, forming an asymmetric channel that opens and allows unidirectional proton passage when the environment of the virus becomes acidic. Due to many previous studies, we now know a great deal about the structural architecture underlying the proton conduction function of the M2 protein, especially the role of two pore-lining gates, the His37 and Trp41 tetrads. However, the conformational dynamics of the M2 proton channel, especially those controlling the rate of its action, have been much less studied, preventing us from achieving a complete understanding of its action mechanism. In this talk, we will discuss our recent efforts in this regards, with a focus on highlighting results obtained with both infrared (IR) and single-molecule fluorescence techniques. Taken together, these results suggest that a large-scale conformational motion near the Trp41 cluster may play a key role in regulating the proton conduction rate of the channel, as it allows more water molecules to fill the cavity below the His37 cluster.<br/> <br/>

Spectroscopic assessment of the conformational dynamics of the M2 proton channel

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.