UC Riverside Undergraduate Research Journal

Influenza viruses cause seasonal epidemics and occasional pandemics around the world. During each flu season, IAV and IBV viruses are circulated widely in the community, with IAV being the dominant circulating virus and IBV accounting for 25% of all flu cases on average. Due to the significant threat posed by the flu virus, international organizations, including the World Health Organization (WHO), have risen to prominence in limiting its global effect. Despite the vaccinations and anti-flu medications that have been develop to combat influenza, drug resistance development highlights the necessity of further studies for influenzas virus pathogenesis and new therapeutic development. Förster resonance energy transfer (FRET) is a technique for detecting protein interactions in vitro and in vivo that is widely employed in biological and biomedical research. Here we report that the IBV M1 protein has a high affinity with human SUMOylation enzymes, the conjugating enzyme UBC9 and the ligase PIAS1, and conform M1 can be SUMOylated determined with a quantitative FRET (qFRET) assay developed in our lab. Understanding the viral infection process and developing new treatment methods requires identifying and deciphering the host route of viral infection. It is critical to comprehend the viral infection process and develop new therapeutics. Blocking the host human SUMOylation pathway is particularly effective for IBV reduction. Our research provides a direct interaction of human proteins with influenza B protein, providing new insights in human-virus interactions for future therapeutics development.