Observational analysis identifies HLA-DRB1*15:01 restricted epitopes in autoantigens, suggesting low bacterial prevalence of similar peptides.
Immunogenicity plays a crucial role in the pathogenesis of autoimmune neuropathy associated with MOG and AQP4 proteins. Hence, we employed computational tools, including MHC-II Binding Prediction and B Cell Epitope Prediction tools from IEDB, Clustal Omega, SWISS-MODEL, AbodyBuilder, HDOCK, AlphaFold Protein Structure Database, and Protein Data Bank, to identify potential HLA-DRB1*15:01 restricted T-cell and B-cell epitopes of the autoantigens MOG and AQP4 and their structural characteristics. Subsequently, the peptide sequences of bacterial proteins identical to the epitopes of MOG and AQP4 proteins were analyzed using BLASTp, MoRFchibi SYSTEM, IUPred3, SEG, miPepBase, and NCBI databases to detect the presence of MoRF, SliM, and LCR. Our findings revealed that MOG22-LQVSSSY-28, MOG80-YRNGKD-85, MOG179-QYRLRGKL-186 and AQP475-CTRKIS-80 were common sequences of the HLA-DRB1*15:01 restricted T-cell and B-cell epitopes of the autoantigens MOG and AQP4. While MoRFs and LCRs were found in some bacteria, the prevalence was low (10.81% and 5.40%, respectively). This suggests that these bacteria may not use the identical peptides to regulate protein-protein interactions and host cell activities.
No takes yet. Share an insight, caveat, or question.
Nhan et al. (2026) studied this question.
Synapse has enriched 5 related papers. Consider them for comparative context: