Study Hydrophobicity and Antigenicity of Cytochrome C Oxidase Subunit II from D. medinensis: New Prototype of Synthetic Vaccine Development
Sonu Mishra and Virendra S Gomase*
Department of Biotechnology, Mewar University, Chittorgarh, India
- *Corresponding Author:
- Virendra S. Gomase
Department of Biotechnology
E-mail: [email protected]
Received date: December 11, 2015; Accepted date: January 07, 2016; Published date: January 12, 2016
Citation: Mishra S, Gomase VS (2016) Study Hydrophobicity and Antigenicity of Cytochrome C Oxidase Subunit II from D. medinensis: New Prototype of Synthetic Vaccine Development. Immunochem Immunopathol 2:113. doi:10.4172/2469-9756.1000113
Copyright: © 2016 Mishra S, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Cytochrome c oxidase subunit II, also known as cytochrome c oxidase polypeptide II which is an oligomeric enzyme. In this study Cytochrome c oxidase subunit 2 (mitochondrion) protein has been used to investigate its role in antigenicity. Cytochrome c oxidase subunit 2 protein sequences (230 aa protein) is analyzed through different types B- cell epitope prediction methods. We found that the region of maximal hydrophilicity is likely to be an antigenic site, having hydrophobic characteristics, because the terminal regions of antigen protein is solvent accessible and unstructured, antibodies against those regions are also likely to recognize the native protein. It was seen that an antigen protein is hydrophobic in nature and contains segments of low complexity and high-predicted flexibility. The predicted antigenic protein segments of Cytochrome c oxidase subunit 2 can take active part in the host immune reactions. In future study the predicted antigenic protein Cytochrome c oxidase subunit 2 fragments can be used in the investigation of MHC molecules binding and it can be the first bottlenecks in vaccine design.