Toward a PA-Inhibitor Complex Crystal System: Influenza Polymerase Acidic Protein Fusion Constructs and Protein Expression

Author(s)

Rebecca Kramb, University of Dayton

Advisor

Doug Daniels

Department

Chemistry

Publication Date

4-26-2020

Document Type

Honors Thesis

Abstract

Globally, three to five million people are afflicted on a yearly basis with serious illnesses due to influenza. In attempts to combat this epidemic, vaccines and antivirals are developed, yet they are not effective enough. The polymerase acidic protein (PA) is vital for viral replication, and inhibiting PA would potentially stop the virus from replicating. In order to inhibit PA effectively, the structure of the protein inhibition site is beneficial but has not yet been obtained because the site is blocked by another protein in crystal structures. Our solution is to fuse different proteins to PA to open up the structure to allow visualization of PA-inhibitor complexes. Various molecular biology techniques were used to create 18 different DNA constructs that were then transformed into bacterial cell lines to be expressed as protein.

Permission Statement

This item is protected by copyright law (Title 17, U.S. Code) and may only be used for noncommercial, educational, and scholarly purposes.

Keywords

Undergraduate research

eCommons Citation

Kramb, Rebecca, "Toward a PA-Inhibitor Complex Crystal System: Influenza Polymerase Acidic Protein Fusion Constructs and Protein Expression" (2020). Honors Theses. 264.
https://ecommons.udayton.edu/uhp_theses/264