Collection, annotation and analysis of peptides and immune epitopes in cancer vaccines targeting MUC1 – UROP Spring Symposium 2025

Collection, annotation and analysis of peptides and immune epitopes in cancer vaccines targeting MUC1

Olena Zhmuryk

Research Mentor(s): Yongqun He
Mentor Department:
Authors: Olena Zhmuryk, Yongqun (Oliver) He
Session: Session 7 (4:00pm – 4: 50pm)
Presentation Type: Poster 9

Abstract

The VIOLIN vaccine database currently includes 4,712 vaccines or vaccine candidates from 219 pathogens. Within VIOLIN, CanVaxKB functions as a cancer vaccine knowledgebase, compiling data on 807 cancer vaccines, including canvaxgens, epitopes, and peptide sequences. Canvaxgens encode proteins or peptides used in cancer vaccines. Peptides are preferred over whole proteins for their higher specificity. Epitopes are peptides that elicit specific immune responses. However, the patterns governing their efficacy in cancer vaccine antigens remain unclear, representing a key area of cancer immunotherapy research. MUC1 is a transmembrane glycoprotein that plays a crucial role in epithelial protection and immune modulation, but in cancers such as breast, pancreatic, and ovarian, it becomes overexpressed, abnormally glycosylated, and loses its apical polarity, leading to the exposure of tumor-associated epitopes. These changes make MUC1 a promising target for cancer immunotherapy. Manual collection and annotation of MUC1 cancer vaccines were conducted from peer-reviewed papers and clinical trials and added to the CanVaxKB database. For some of the vaccines, the epitope information was identified, particularly for those found on Cancer Epitope Database and Analysis Resource (CEDAR). Other major MUC1 epitopes were identified from peer-reviewed papers. Bioinformatics analysis was then conducted. It was concluded that the immunogenicity of MUC1 epitopes is influenced by their specific amino acid composition and interaction with MHC molecules and immune receptors. Amino acids, including proline, arginine, aspartic acid, threonine, and serine, play essential roles in epitope stability, MHC binding affinity, and T-cell activation, with modifications in these residues affecting immune recognition. Five key MUC1 epitopes were identified: SAPDTRPAPG, PDTRPAP, RPAPGS, STAPPAHGV, and LLLLTVLTV. HLA-A2 and HLA-A11 binding epitopes should be prioritized for cytotoxic T-cell response induction. These findings enhance our understanding of the biomolecular mechanisms behind MUC1 cancer vaccines and emphasize the need for careful epitope selection to develop more effective therapies.

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