Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.

ABSTRACT: The M2 proton channel of the influenza A virus has been the subject of extensive studies because of its critical role in viral replication. As such, we now know a great deal about its mechanism of action, especially how it selects and conducts protons in an asymmetric fashion. The conductance of this channel is tuned to conduct protons at a relatively low biologically useful rate, which allows acidification of the viral interior of a virus entrapped within an endosome, but not so great as to cause toxicity to the infected host cell prior to packaging of the virus. The dynamic, structural and chemical features that give rise to this tuning are not fully understood. Herein, we use a tryptophan (Trp) analog, 5-cyanotryptophan, and various methods, including linear and nonlinear infrared spect

SUBMITTER: Markiewicz BN 

PROVIDER: S-EPMC5157935 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature