The duality of [Fe-S] and Zn cofactors in viral proteins

Many viral proteins are intrinsically disordered and often annotated as non structural proteins. These comprise elemental components of viruses, such as Sars-Cov2, PRRSV, Hepatitis, etc. for the viruses to replicate and efficiently infect the host. Many of these proteins contain conserved cysteines and histidines that can act as ligands for metallocofactors, such as Zn and [Fe-S] clusters. In fact, many of these proteins have been annotated as Zinc Finger proteins, because they contain a variable CCCH motif. Our research demonstrates that many of these proteins can in addition accomodate an [Fe-S] cofactor, the latter of which in many cases is the physiological cofactor. We have embarged onto a functional and structural journey to indentify such proteins and characterize their cofactors. The outcomes of this research will have many implications for the treatment of viral-related diseases and developement of therapeutic targets.