Measurement of Proton Flux through Influenza A Viral Protein M2

Authors

J. Craig Moffat, Brigham Young University
Matthew A. D'Haenens, Brigham Young University
David D. Busath, Brigham Young University
Dr. Dixon J. Woodbury, Brigham Young University

Keywords

proton flux, influenza A, protein M2

College

Life Sciences

Department

Physiology and Developmental Biology

Abstract

The Influenza A viral protein M2 is known to conduct protons across viral, Golgi, and cell membranes. M2 allows acidification of the interior of the virion thus facilitating viral RNA uncoating. In the active form, M2 is a homotetramer. Each subunit consists of 97 amino acid residues with only one membrane-spanning region of 19 residues. The ion channel activity of M2 has been studied at physiological pH in cellular systems. It is also known that the channel is sensitive to the anti-influenza drug amantadine. Understanding M2 activity at pH 7 will give us greater knowledge of viral function, pharmacological sensitivities, and will allow researchers to understand more complex proton channels.

Recommended Citation

Moffat, J. Craig; D'Haenens, Matthew A.; Busath, David D.; and Woodbury, Dr. Dixon J. (2013) "Measurement of Proton Flux through Influenza A Viral Protein M2," Journal of Undergraduate Research: Vol. 2013: Iss. 1, Article 1403.
Available at: https://scholarsarchive.byu.edu/jur/vol2013/iss1/1403