Biophysical Studies of a Protein of Unknown Function from Cancer‐Associated Murine Herpesvirus‐68

Abstract

Members of the Herpesvirus family cause several types of diseases to its mammalian hosts, including infectious mononucleosis, Hodgkin’s lymphoma, and primary effusion lymphomas. Herpesviruses are characterized by their ability to replicate and spread infection in the active lytic phase, but also maintain themselves within a host during the inactive latent phase. Within the gammaherpesvirus subfamily, a conserved protein of unknown function, with a highly conserved domain of unknown function, is expressed during the lytic phase. The protein was observed to be essential to viral replication during the lytic phase of infection when the gene was knocked out of the murine gammaherpesvirus‐68 (MHV68). To characterize its biophysical properties, the protein of unknown function from MHV68 was purified. Analysis of the protein through Circular Dichroism spectroscopy determined the secondary structure to be predominantly alpha‐helical. The thermal denaturation of the protein was pH dependent. Additionally, using a high throughput screen, the thermal stability of the protein was increased in the presence of small organic acids. The goal of the biophysical and structural analyses is to identify the function of the protein in the viral life cycle and to determine if the protein can be targeted to inhibit replication of gammaherpesviruses and their associated diseases.Support or Funding InformationThis work was supported by UWL College of Science and Health, UWL Undergraduate Research and Creativity, and Hardy W. Chan and Sons Chemistry Summer Undergraduate Research Fellowship.