1.Department of General Surgery, the First Affliated Hospital of Wenzhou Medical University, Wenzhou, 325015; 2.Department of Microbiology and Immunology, Institute of Molecular Virology and Immunology, Institute of Tropical Medicine, Wenzhou Medical University, Wenzhou, 325035
CHEN Xudong,CHENG Kai,LYU Kaiji, et al. Analysis and predication of B cell epitopes of programmed cell death ligand 1[J]. JOURNAL OF WEZHOU MEDICAL UNIVERSITY, 2018, 48(1): 7-12,19.
Abstract：Objective: To predict and screen the B-cell epitopes of the programmed cell death ligand 1 (PD-L1), in the hope of being used in the research of antagonist to block the protein-protein interaction between the transmembrane protein programmed cell death protein 1 (PD-1) and its ligand. Methods: Base on the full-length amino acid sequence of human and mouse PD-L1, the B-cell epitopes of the PD-L1 were predicted by bioinformatics method, including the secondary structure, the hydrophilic plot technique, polarity parameters, surface probability, and the antigenic index. Along with molecular modeling and functional mapping, antigenic index calculation was further taken as a standard to determine target epitopes. The amino acid sequence alignment of the predicted B epitopes of PD-L1 was blasted with other four kinds of experimental animal PD-L1. Results: Human and mouse PD-L1 was a 33 kDa type I membrane protein consisting of 290 amino acids. Extracellular part of human and mouse PD-L1 was at 19-238 and 19-239 respectively. The predicted B-cell epitopes of human and mouse PD-L1’s which could be used in the research of antagonist to block the protein-protein interaction between PD-1 and PD-L1’s might exist in N-terminal of amino acid sequence: 41-46 (KFPVEK), 60-63 (EDKN), 71-75 (EEDLK) and 40-48 (RFPVERELDL), 58-63 (EKEDE), 72-88 (EDLKPQH) respectively. Homology analysis showed the amino acid sequence (41-50, 58-62, 71-80) which contains the predicted B-cell epitopes was highly conservative in different species. Conclusion: Bioinformatic prediction along with molecular modeling and functional mapping which concludes in three amino acid seuences each for human and mouse provides a theoretical basis for further study of antagonist to block the protein-protein interaction between PD-1 and PD-L1.
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