Changes in Interaction Between Accessory Protein 8 and IL-17RA in UK Isolates Caused by Mutations in the SARS-CoV-2 Open Reading Frame 8

SARS-CoV-2 is the infectous agent of Covid-19, one most important health problems twenty-first century. IL-17RA an crucial receptor in generation host immune response. ORF8 viral accessory protein that suppresses Mutations can alter properties and clinical course SARS-CoV-2. In this study, we investigated changes mutations may cause interaction with ORF8. The study was carried out using 825 complete genome sequences from UK isolates. Mutation analyzes were performed RDP4 MEGAX. model created Swiss Model. Protein analyzed by Haddock ver 2.4. Analysis stability SDM2, mCSM DUET tools. change - binding affinity before after mutation evaluated mCSM-PPI2. We detected P30S, R52I, Y73C L118V have been shown to reduce affinity. After mutation, dynamics changed. Molecular attachment scores -78.0±3.4 kcal.mol-1 -76.3±11.9 kcal.mol-1, for wild type mutant, respectively. mutations, hydrogen bond number position between While establishing ten bonds IL-17RA, four established mutant IL-17RA. decreased be seen as a stronger response milder course. Although our results contain data understanding ORF8, which drug target, it needs repeated in-vivo crystallgraphy studies.