Insilico Validation of Babesia Bovis Merozoite Surface Antigen-1, Merozoite Surface Antigen-2b and Merozoite Surface Antigen-2c Proteins for Vaccine and Drug Development

The Babesia bovis MSA-1, MSA-2b and MSA-2c are members of the variable merozoite surface antigen (VMSA) family, they are encoded surface proteins that are proposed to mediate the initial attachment of the merozoite to the host erythrocyte so this protein are targeted for vaccine and drug design. So the aim of this study is to give an outlook for MSA-1, MSA-2b and MSA-2c proteins using bioinformatics tools to help the developing drug and vaccine. In the present study, an in silico techniques were initiated to characterize the properties and structure of the MSA-1, MSA-2b and MSA-2c proteins. Firstly, the Physico-chemical characterization were computed by ExPasy’s (ProtParam). Then the functional site prediction was done using ScanProsite. Subsequently, for functional characterization were computed the transmembrane regions and phosphorylation sites by SOSUI server and NetPhos server respectively. Thereafter, secondary structure prediction was explored using GOR IV. Finally, the 3D structure of proteins was built by sequence homology using CPH models 3.2 servers envision by Chimera 1.8 programming. The model was further surveyed by ERRAT, this confirmation of the quality of the model. Our results revealed that MSA-2c may be stable for a wide range of temperatures and the MSA-1 and MSA-2b classified as an unstable protein. While the MSA-2b less stable in test tube than MSA-2c and MSA-1. Further, all proteins are acidic and hydrophilic in nature, negatively charged, membrane and serine is the most phosphorylated amino acid in the Proteins. Also, we detected the sequences belonging to the following families: ASN_GLYCOSYLATION, CK2_PHOSPHO_SITE, PKC_PHOSPHO_SITE, MYRISTYL and TYR_PHOSPHO_. The secondary structure prediction of these proteins revealed that MSA-1, MSA-2b and MsA-2c have predominant mixed secondary structures. The 3 D structure for proteins were modeling and we found the quality of 3D structures less than 90%. Based on the findings, it could be concluded that further characterization of the Babesia bovis proteins is novel and will be important for drug and vaccine designing or understanding the interactions between proteins.