In-silico characterization of LSDV132 protein divulged its BCL-2-like nature

Abstract

Lumpy skin disease virus (LSDV) belongs to Poxviridae family. This virus possesses various proteins which impart potential functions to it including assembly of newly synthesized viruses in the replication cycle and forming their structure. LSDV132 protein is also one of such proteins. Its key characteristics were unknown because, no any relevant study was reported about it. This study aimed to investigate its characteristic features and essential functions using several bioinformatics techniques. These analyses included physiochemical characterization and exploring the crucial functional and structural perspectives. Upon analysis of the physiochemical properties, the instability index was computed to be 30.89% which proposed LSDV132 protein to be a stable protein. Afterwards, the phosphorylation sites were explored. Several sites were found in this regard which led to the hypothesis that it might be involved in the regulation of apoptosis and cell signaling, among other cellular processes. Furthermore, the KEGG analysis and the analysis of protein family classification confirmed that the LSDV132 protein possessed Poxvirus-BCL-2-like motifs, indicating that it might be responsible in modulating the apoptosis of host cells. This crucial finding suggested that the protein under study possessed BCL-2-like features. Proceeding this very important finding, the molecular docking analysis was performed. In this context, various viral BCL-2 inhibitors were retrieved from the ChEMBL database for docking purpose. The docking results revealed that pelcitoclax exhibited best docking scores i.e., −9.1841 kcal/mol, among all of the other docked complexes. This fact signified that this compound might serve as an inhibitor of LSDV132 protein.