Proteasomal cleavage site prediction of protein antigen using BP neural network based on a new set of amino acid descriptor.

The accurate identification of cytotoxic T lymphocyte epitopes is becoming increasingly important in peptide vaccine design. The ubiquitin-proteasome system plays a key role in processing and presenting major histocompatibility complex class I restricted epitopes by degrading the antigenic protein. To enhance the specificity and efficiency of epitope prediction and identification, the recognition mode between the ubiquitin-proteasome complex and the protein antigen must be considered. Hence, a model that accurately predicts proteasomal cleavage must be established. This study proposes a new set of parameters to characterize the cleavage window and uses a backpropagation neural network algorithm to build a model that accurately predicts proteasomal cleavage. The accuracy of the prediction model, which depends on the window sizes of the cleavage, reaches 95.454% for the N-terminus and 95.011% for the C-terminus. The results show that the identification of proteasomal cleavage sites depends on the sequence next to it and that the prediction performance of the C-terminus is better than that of the N-terminus on average. Thus, models based on the properties of amino acids can be highly reliable and reflect the structural features of interactions between proteasomes and peptide sequences.