Abstract
Eimeria acervulina is a species of Eimeria that causes coccidiosis in older poultry. Lesions are limited to anterior or first third of the small intestine . 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 Eimeria acervulina are important determinant for protection of host form parasitic infection. In this assay, we used PSSM and SVM algorithms for antigen design and predicted the binding affinity of antigen protein having 299 amino acids, which shows 291 nonamers. Binding ability prediction of antigen peptides to major histocompatibility complex (MHC) class I & II molecules is important in vaccine development from Eimeria acervulina . Keywords - antigen protein, epitope, PSSM, SVM, MHC, peptide vaccine
Highlights
Eimeria acervulina is a species of Eimeria that causes coccidiosis in older poultry
Eimeria acervulina antigen peptides are most suitable for subunit vaccine development because with single epitope, the immune response can be generated in large population
We found the SVM based MHCII-IAb peptide regions; MHCII-IAd peptide regions; MHCII-IAg7 peptide regions and MHCII- RT1.B peptide regions, which represented predicted binders from bacterial antigen protein (Table 2)
Summary
Eimeria acervulina is a species of Eimeria that causes coccidiosis in older poultry. Eimeria acervulina antigen peptides are most suitable for subunit vaccine development because with single epitope, the immune response can be generated in 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 Eimeria acervulina is necessary for new paradigm of synthetic vaccine development and target validation [3,4,5]
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