EPCES
EPCES predicts antigen epitopes by integrating six scoring functions to identify potential epitopic regions on proteins for immunological and therapeutic applications.
Key Features:
- Consensus scoring: Combines multiple computational strategies into a consensus approach to improve epitope prediction accuracy.
- Residue epitope propensity: Scores residue-level propensity to belong to an epitope.
- Conservation score: Evaluates sequence conservation to identify epitopes conserved across strains or variants.
- Side-chain energy score: Assesses side-chain interaction energies influencing epitope stability.
- Contact number: Measures residue contact number to reflect exposure and local interaction density.
- Surface planarity score: Quantifies surface planarity relevant to epitope accessibility.
- Secondary structure composition: Incorporates secondary structure composition as a factor in epitope prediction.
- Candidate prioritization: Ranks and prioritizes candidate epitopes based on the combined scoring metrics.
- Identification of conserved and functionally relevant regions: Detects epitopic regions that are conserved and likely functionally important.
- Epitope accessibility and immunogenicity: Pinpoints epitopes that are accessible and likely to be immunogenic for antibody development.
Scientific Applications:
- Vaccine design: Identifies conserved and relevant epitopes to support rational design of vaccines targeting multiple strains or variants.
- Monoclonal antibody development: Pinpoints accessible and immunogenic epitopes for antibody targeting.
- Autoimmune disease studies: Predicts epitopes associated with self-antigens to inform autoimmune research.
- Cancer immunotherapy: Predicts tumor antigen epitopes to support development of targeted therapies and personalized medicine approaches.
Methodology:
Consensus approach combining six scoring functions: residue epitope propensity, conservation score, side-chain energy score, contact number, surface planarity score, and secondary structure composition.
Topics
Details
- Tool Type:
- command-line tool
- Added:
- 12/18/2017
- Last Updated:
- 11/25/2024
Operations
Publications
Liang S, Liu S, Zhang C, Zhou Y. A simple reference state makes a significant improvement in near‐native selections from structurally refined docking decoys. Proteins: Structure, Function, and Bioinformatics. 2007;69(2):244-253. doi:10.1002/prot.21498. PMID:17623864. PMCID:PMC2673351.