Date of Award

Spring 2019

Document Type


Terms of Use

© 2019 Abigail J. Wong-Rolle. All rights reserved. This work is freely available courtesy of the author. It may only be used for non-commercial, educational, and research purposes. For all other uses, including reproduction and distribution, please contact the copyright holder.

Degree Name

Bachelor of Arts


Chemistry & Biochemistry Department

First Advisor

Kathleen P. Howard


Influenza A presents a significant concern for public health as it is the cause of seasonal outbreaks and global pandemics. The influenza A proteins, matrix protein 1 (M1) and matrix protein 2 (M2), have been shown to be essential for the propagation of new viruses, especially through their roles in viral assembly and budding. The M2 cytoplasmic tail interacts with the M1 protein, recruiting it to the viral budding site and enabling proper packaging of the viral genome. The Howard lab has previously characterized residues 50-70 in the M2 cytoplasmic tail and the M2 protein’s conformational equilibria by sitedirected spin label electron paramagnetic resonance (SDSL-EPR). This work lays groundwork for the establishment of a system in which to see changes in the M2 protein upon M1 binding. Methods for the overexpression and purification of the M1 protein are presented. Selected M2 sites (43, 57, 68) were studied by SDSL-EPR in the presence of Nterminal M1 (residues 1-165), with M2 sites 43 and 57 acting as indicators of the M2 protein’s conformational dynamics. Binding between M1 and M2 could not be rigorously established, but preliminary results suggest little change in the M2 protein in the presence of the M1 protein.

Included in

Chemistry Commons