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Title: Biophysical studies on influenza A M2 protein
Author: Duff, Kevin Campbell
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 1993
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The influenza A M2 protein and, in particular, the proposed transmembrane domain, has been implicated in viral infectivity at two stges in the replicative cycle: viral uncoating and assembly. An identical function has been proposed for the protein at both points of interest, that is, that M2 acts as a proton channel. In order to work, this hypothesis assumes that M2 possesses a transmembrane domain, presumably in a α-helical conformation, that this domain orientates in a prescribed manner across the bilayer and that, indeed, M2 is able to translocate protons across the aforementioned bilayer. This thesis examines these assumptions experimentally using a synthetic, 25 amino acid peptide representing the proposed transmembrane domain of M2. The work described herein may be divided into three main areas, each employing a separate biophysical technique. Circular dichroism was employed to assign an α-helical secondary structure to the M2 peptide. Neutron diffraction orientated this region precisely in the bilayer. Electrophysiological techniques observed directly, for the first time in viruses, proton translocation. The effects of amantadine, the only drug prescribed for use against influenza A infections, in each of these structural asnd functional investigations has also been recorded, providing revealing insights into the drug's efficacy. M2 has structural analogs in other enveloped viruses and work such as that reported in this thesis may reveal a common pathway of viral infectivity for groups of enveloped viruses, therefore allowing the possibility of broad-spectrum drug therapies.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available