Date of Award

2020

Degree Type

Thesis

Degree Name

Honors Thesis

Department

Biology

First Advisor

Christopher Stobart

Abstract

Human coronaviruses are responsible for a number of physiological ailments and include illnesses such as the common cold, Middle East Respiratory Syndrome (MERS), Severe Acute Respiratory Syndrome (SARS), pneumonia, and COVID-19. While vaccines exist for a multitude of pathogenic viruses that exists today, human coronaviruses are not among those that possess a stable and efficacious vaccine available on the market. Attempts to make an inhibitor against coronaviruses have targeted the active site and substrate binding sites of a protease known as non-structural protein 5 (Nsp5), however these attempts have failed to date. Models of the structure of MHV Nsp5 show a high level of similarities to the Nsp5 structures of human clinical strains such as HKU1, OC43, NL63, and 229E that combine to cause the common cold 8,10. There are also a high level of similarities to the Nsp5 stucture to the more recently discovered SARS-CoV-2. A unique loop region found between two structural domains of the protease Nsp5 called the interdomain loop (IDL) has been poorly characterized. In this study, I aim to determine the role of the MHV IDL through the analysis of a series of viral mutations introduced throughout the IDL region of the virus.

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