Enhancement of conformational B-cell epitope prediction using CluSMOTE

Background. A conformational B-cell epitope is one of the main components of vaccine design. It contains separate segments in its sequence, which are spatially close in the antigen chain. The availability of Ag-Ab complex data on the Protein Data Bank allows for the development predictive methods. Several epitope prediction models also have been developed, including learning-based methods. However, the performance of the model is still not optimum. The main problem in learning-based prediction models is class imbalance. Methods. This study proposes CluSMOTE, which is a combination of a clusterbased undersampling method and Synthetic Minority Oversampling Technique. The approach is used to generate other sample data to ensure that the dataset of the conformational epitope is balanced. The Hierarchical DBSCAN algorithm is performed to identify the cluster in the majority class. Some of the randomly selected data is taken from each cluster, considering the oversampling degree, and combined with the minority class data. The balance data is utilized as the training dataset to develop a conformational epitope prediction. Furthermore, two binary classification methods, Support Vector Machine and Decision Tree, are separately used to develop model prediction and to evaluate the performance of CluSMOTE in predicting conformational B-cell epitope. The experiment is focused on determining the best parameter for optimal CluSMOTE. Two independent datasets are used to compare the proposed prediction model with state of the art methods. The first and the second datasets represent the general protein and the glycoprotein antigens respectively. Result. The experimental result shows that CluSMOTE Decision Tree outperformed the Support Vector Machine in terms of AUC and Gmean as performance measurements. The mean AUC of CluSMOTE Decision Tree in the Kringelum and the SEPPA 3 test sets are 0.83 and 0.766, respectively. This shows that CluSMOTE Decision Tree is better than other methods in the general protein antigen, though comparable with SEPPA 3 in the glycoprotein antigen.