iPVP-MCV: A Multi-Classifier Voting Model for the Accurate Identification of Phage Virion Proteins

The classic structure of a bacteriophage is commonly characterized by complex symmetry. The head of the structure features icosahedral symmetry, whereas the tail features helical symmetry. The phage virion protein (PVP), a type of bacteriophage structural protein, is an essential material of the infectious viral particles and is responsible for multiple biological functions. Accurate identification of PVPs is of great significance for comprehending the interaction between phages and host bacteria and developing new antimicrobial drugs or antibiotics. However, traditional experimental approaches for identifying PVPs are often time-consuming and laborious. Therefore, the development of computational methods that can efficiently and accurately identify PVPs is desired. In this study, we proposed a multi-classifier voting model called iPVP-MCV to enhance the predictive performance of PVPs based on their amino acid sequences. First, three types of evolutionary features were extracted from the position-specific scoring matrix (PSSM) profiles to represent PVPs and non-PVPs. Then, a set of baseline models were trained based on the support vector machine (SVM) algorithm combined with each type of feature descriptors. Finally, the outputs of these baseline models were integrated to construct the proposed method iPVP-MCV by using the majority voting strategy. Our results demonstrated that the proposed iPVP-MCV model was superior to existing methods when performing the rigorous independent dataset test.

Automated summary

The classic structure of a bacteriophage exhibits complex symmetry with icosahedral symmetry in the head and helical symmetry in the tail. The phage virion protein (PVP) plays a crucial role in viral infection and understanding the interaction between phages and host bacteria. Developing computational methods, such as the iPVP-MCV model, can efficiently and accurately identify PVPs for potential antimicrobial drug development.