International Journal of Bioinformatics and Biomedical Engineering
Articles Information
International Journal of Bioinformatics and Biomedical Engineering, Vol.2, No.1, Jan. 2016, Pub. Date: Jan. 18, 2016
Insilico Validation of Babesia Bovis Merozoite Surface Antigen-1, Merozoite Surface Antigen-2b and Merozoite Surface Antigen-2c Proteins for Vaccine and Drug Development
Pages: 30-39 Views: 1455 Downloads: 1189
[01] Sofia B. Mohamed, Vector and Biomedical Studies, Tropical Medicine Research Institute, Khartoum, Sudan.
[02] Mohamed M. Hassan, Faculty of Medical Laboratory Sciences, Al Zaiem Al Azhari University, Khartoum, Sudan.
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.
Babesia Bovis, MSA-1, MSA-2b, MSA-2c Proteins, Insilico Analysis, Physico-Chemical Character, 3-D Modeling and Functional Characterization
[01] Hines S., McElwain T, Buening G, Palmer G. 1989. Molecular characterization of Babesia bovis merozoite surface proteins bearing epitopes immunodominant in protected cattle. Molecular Biochemical Parasitology. 37: 1–9.
[02] LeRoith T., Brayton A, Molloy J et al. 2005. Sequence variation and immunologic cross-reactivity among Babesia bovis merozoite surface antigen1 proteins from vaccine strains and vaccine breakthrough isolates. Infection And Immunity. 73: 5388–5394.
[03] Brown W., Palmer G. 1999. Designing blood-stage vaccines against Babesia bovis and Babesia bigemina. Parasitol today Journal. 15: 275–281.
[04] Mosqueda J., McElwain T, Palmer G. 2002. Babesia bovis merozoite surface antigen 2 proteins are expressed on the merozoite and sporozoite surface, and specific antibodies inhibit attachment and invasion of erythrocytes. Infection and Immunity. 70: 6448–6455.
[05] Florin-Christensen M., Suarez C, Hines S et al. 2002. The Babesia bovis merozoite surface antigen 2 locus contains four tandemly arranged and expressed genes encoding immunologically distinct proteins. Infection and Immunity journal. 70:3566–3575.
[06] Dubremetz J., Garcia-Reguet N, Conseil V, Fourmaux M. 1998. Apical organelles and host-cell invasion by Apicomplexa. International Journal of Parasitology. 28: 1007–1013.
[07] Suarez, C. E., Laughery, J. M., Bastos, R. G., Johnson, W. C., Norimine, J., Asenzo, G., Brown, W. C., Florin-Christensen, M. and Goff, W. L. 2011. A novel neutralization sensitive and subdominant RAP-1-related antigen (RRA) is expressed by Babesia bovis merozoites. Parasitology 18: 1–10.
[08] Carcy, B., Précigout, E., Schetters, T. and Gorenflot, A. 2006. Genetic basis for GPI-anchor merozoite surface antigen polymorphism of Babesia and resulting antigenic diversity. Veterinary Parasitology. 138: 33–49.
[09] Giancarlo R., Siragusa. A, Siragusa. E. et al. 2007. A Basic Analysis Toolkit for Biological Sequences, Algorithms for Molecular Biology.2: 404-406.
[10] Ashokan.K, Pillai. M. 2008. Characterization of biomimetc material, Mussel adhesive protein, using computer tools and servers. The Internet Journal of Bioengineering. 4: 1-8.
[11] Gay C.G, Zuerner R, Bannantine J.P, Lillehoj H.S, Zhu J.J, Green R. Pastoret P.P. 2007.Genomics and vaccine development Revue scientifique et technique (International Office of Epizootics). 26: 49-67.
[12] Sheoran. S, Pandey. B, Sharma. P, et al. 2013.In silico comparative analysis and expression profile of antioxidant proteins in plants Genetics and Molecular Research. 12: 537-551.
[13] Rost.B, Eyrich. V. 2001. Large-scale analysis of secondary structure prediction. Proteins 45 Suppl. 5: S192–S199.
[14] Prajapati. C, Bhagat. C.2012. In-Silico Analysis and Homology Modeling of Targets Proteins for Clostridium botulinum. International Journal Pharmaceutical sciences and research. 3: 2050-2056.
[15] Mundaganore S., Mundagnore D, Ashokan V. 2013. In Silico Validation OF Middle East Respiratory Syndrome (MERS) Virus Protins For Better Drug Development. International Journal of Applied Sciences and Biotechnology. 1: 272-278.
[16] K. Guruprasad, B. Reddy, M. Pandit. 1990. Correlation between stability of a protein and its dipeptide composition: a novel approach for predicting in vivo stability of a protein from its primary sequence. Protein Engineering. 4: 155-161.
[17] Ikai A. 1980.Thermostability and aliphatic index of globular proteins. Journal of Biochemistry. 88: 1895-1898.
[18] Kyte J and Doolittle R. 1982. A simple method for displaying the hydropathic character of a protein. Journal of Molecular Biology. 157: 105-132.
[19] Castro E. de, Sigrist. C.J., Gattiker. A, et al. 2006. ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins. Nucleic Acids Research.34: 362-365.
[20] Blom. N. Gammeltoft. S, Brunak. S. 1999. Sequence- and structure-based prediction of eukaryotic protein phosphorylation sites. Journal of Molecular Biology. 294: 1351-1362.
[21] Ramachandran G.N, Sasiskharan. V. 1968. Conformation of polypeptides and proteins. Advances in Protein Chemistry 23: 283–437.
[22] Garnier, J., Gibrat, J.F. and Robson B. (1996). GOR secondary structure prediction method version IV. In: R.F. Doolittle (Ed.) Computer Methods for Macromolecular Sequence Analysis, Methods in Enzymology, vol. 266. Academic Press, USA. pp. 540-553.
[23] Mohammed A., Wasal A, Entssar S et al. 2015. Europe Academic of Research. Bioinformatics approach prediction of nonsynonymous and miRNA-binding site polymorphisms within human SclA9 and Scl22A12 genes. Vol II: 15412-15429.
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