Microbial Proteomics Approach for Sensitive Quantitative Predictions of MHC Binding Peptide from Taenia Ovis

Taenia ovis is a tapeworm parasite with the adult stage of the parasite found in the intestines of dogs, while the intermediate or larval stage is found in the muscles of sheep, causes sheep measles. Peptide fragments of antigen protein can be used to select nonamers for use in rational vaccine design, and to increase the understanding of roles of the immune system in infectious diseases. Analysis shows MHC class II binding peptides of antigen protein from Taenia ovis are important determinants for protection of host from parasitic infection. In this assay, we used PSSM and SVM algorithms for antigen design and predicted the binding affinity of antigen protein having 254 amino acids, which shows 246 nonamers. Binding ability prediction of antigen peptides to Major Histocompatibility Complex (MHC) class I & II molecules is important in vaccine development against sheep measles. ProtScale output for user sequence 3


Introduction
Taenia ovis are the smallest nematode parasite of sheep, are responsible for ovine cysticercosis (Sheep Measles), have an unusual life cycle, and are one of the most widespread and clinically important parasites in the world [1,2]. The small adult worms mature in the intestines of an intermediate host, such as a dog [1,2]. Taenia ovis antigen peptides are most suitable for subunit vaccine development, because with single epitope the immune response can be generated in a large population. This approach is based on the phenomenon of cross-protection, whereby infected with a mild strain and is protected against a more severe strain of the same. The phenotype of the resistant transgenic hosts includes fewer centers of initial infection, a delay in symptom development and low accumulation. Antigen protein from Taenia ovis is necessary for new paradigm of synthetic vaccine development and target validation [3][4][5].

Virendra Gomase* and Chitlange NR
The Global Open University, Nagaland, India

Abstract
Taenia ovis is a tapeworm parasite with the adult stage of the parasite found in the intestines of dogs, while the intermediate or larval stage is found in the muscles of sheep, causes sheep measles. Peptide fragments of antigen protein can be used to select nonamers for use in rational vaccine design, and to increase the understanding of roles of the immune system in infectious diseases. Analysis shows MHC class II binding peptides of antigen protein from Taenia ovis are important determinants for protection of host from parasitic infection. In this assay, we used PSSM and SVM algorithms for antigen design and predicted the binding affinity of antigen protein having 254 amino acids, which shows 246 nonamers. Binding ability prediction of antigen peptides to Major Histocompatibility Complex (MHC) class I & II molecules is important in vaccine development against sheep measles.  region in putative antigen protein (Table 1). Additionally, SVM based MHCII-IAb peptide regions were also found; MHCII-IAd peptide regions; MHCII-IAg7 peptide regions and MHCII-RT1.B peptide regions were also found, which represented predicted binders from bacterial antigen protein ( Table 2). The predicted binding affinity is normalized by the 1% fractal. Through this study, an improved method for predicting linear epitopes has been described ( Table 2). The region of maximal hydrophilicity is likely to be an antigenic site, having hydrophobic characteristics (Figure 1-4), because terminal regions of antigen protein is solvent accessible and unstructured; antibodies against those regions are also likely to recognize the native protein ( Figure 5-7). It was shown that an antigen protein is hydrophobic in

Results and Interpretations
Binding of peptides to a number of different alleles using Position Specific Scoring Matrix have been found through this study. An antigen protein sequence is 254 residues long having antigenic MHC binding peptides. MHC molecules are cell surface glycoproteins, which take active part in host immune reactions and involvement of MHC class-I and MHC II in response to almost all antigens. PSSM based server predict the peptide binders to MHCI molecules of antigen protein sequence which are as 11mer_H2_Db, 10mer_H2_Db, 9mer_H2_Db, 8mer_H2_Db, and also peptide binders to MHCII molecules of antigen protein sequence as I_Ab.p, I_Ad.p; analysis found antigenic epitopes        nature and contains segments of low complexity and high-predicted flexibility (Figure 8-10). Predicted antigenic fragments can bind to MHC molecule, and is the first bottlenecks in vaccine design ( Figure  1-4).

Conclusion
An antigen protein from Taenia ovis peptide nonamers are from a set of aligned peptides known to bind to a given MHC molecule as the predictor of MHC-peptide binding. MHCII molecules bind peptides in similar yet different modes, and alignments of MHCII-ligands were obtained to be consistent with the binding mode of the peptides to their MHC class; this means the increase in affinity of MHC binding peptides may result in enhancement of immunogenicity of antigen protein. These predictions of antigen protein, antigenic peptides to MHC class molecules are important in vaccine development from Taenia ovis.