Cytochrome B - Analysis of Hydrophobicity, Surface Accessibility, Antigenicity and Prediction of MHC I and MHC II Binders from Dracunculiasis
Sonu Mishra and Virendra S Gomase*
Department of Biotechnology, Mewar University, Chittorgarh, India
- *Corresponding Author:
- Virendra S. Gomase
Department of Biotechnology
Mewar University, Chittorgarh, India
E-mail: [email protected]
Received date: December 09, 2015; Accepted date: January 15, 2016; Published date: January 19, 2016
Citation: Mishra S, Gomase VS (2016) “Cytochrome B”- Analysis of Hydrophobicity, Surface Accessibility, Antigenicity and Prediction of MHC I and MHC II Binders from Dracunculiasis. Med chem 6:041-046. doi:10.4172/2161-0444.1000322
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.
In this study, Cytochrome b (mitochondrion) protein has been used to investigate its role in antigenicity. Cytochrome b (mitochondrion) protein sequences (367 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 b (mitochondrion) can take active part in the host immune reactions. In this research, we have also used PSSM and SVM algorithms for the prediction of MHC class I and II binding peptide, antigenicity, Solvent accessibility, polar and nonpolar residue to analyse the regions that are likely exposed on the surface of proteins which are potentially antigenic that allows potential drug targets to identify active sites against infection as well as to design effective drug for treatment.