Date of Award

Spring 2020

Document Type


Terms of Use

© 2020 Elizabeth A. Erler. 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 remains a serious global health threat and further characterization of key viral proteins is necessary in order to develop novel drugs and vaccines. Matrix protein 1 (M1) and matrix protein 2 (M2) of Influenza A Virus play key roles in the assembly and release of new infectious viral particles. The cytoplasmic tail of M2 has been shown to be critical for inducing membrane curvature in order to facilitate budding. M1 has multiple roles, including packaging viral RNA and recruiting it to the budozone through interactions with M2 and other viral membrane proteins. In this role as an adaptor protein, Ml participates in interactions with the membrane, viral genome elements and other viral proteins and it is important to use a full-length M1 construct that is capable of recapitulating these many interactions. In this study, we present an optimized expression and purification protocol for full-length Ml. We also present preliminary data showing characterization of full-length M1 using circular dichroism spectroscopy as well as isothermal titration calorimetry and biolayer interferometry to study Ml-M2 binding.

Included in

Chemistry Commons