The putative metal-binding proteome of the coronaviridae family.

Metalloproteins are well-known for playing various physicochemical processes in all life forms, including viruses. Some life-threatening viruses (such as some members of the coronaviridae family of viruses) are emerged and remerged frequently and are rapidly transmitted throughout the globe. This study aims to identify and characterize the metal-binding proteins of the coronaviridae family of viruses and further provides insight into the metal-binding protein's role in sustaining and propagating viruses inside a host cell and in the outer environment. In the present study, the available proteome of the coronaviridae family was exploited. Identified potential metal-binding proteins were analyzed for their functional domains, structural aspects, and sub-cellular localization. We also demonstrate phylogenetic aspects of all predicted metal-binding proteins among other coronaviridae family members to understand the evolutionary trend among their respective hosts. A total of 256 proteins from 51 different species of coronaviruses are predicted as metal-binding proteins. These metal-binding proteins perform various key roles in the replication and survival of viruses within the host cell. Cysteine, aspartic acid, threonine, and glutamine are key amino acid residues interacting with respective metal ions. Our observations also indicate that the metalloproteins of this family of viruses circulated and evolved in different hosts, which supports the zoonotic nature of coronaviruses. The comprehensive information on metal-binding proteins of the coronaviridae family may be further helpful in designing novel therapeutic metalloprotein targets. Moreover, the study of viral metal-binding proteins can also help to understand the roles of metal-binding proteins in virus pathogenesis and virus-host interactions.