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Updated: Dec 13, 2025

A High Throughput MHC II Binding Assay for Quantitative Analysis of Peptide Epitopes
Published on: March 25, 2014
Vaccine candidate designed against carcinoembryonic antigen-related cell adhesion molecules using immunoinformatics
Aditya Gupta1, Andrew J Rosato1, Feng Cui1
1Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, Rochester, NY, USA.
Abstract:
Carcinoembryonic antigen-related cell adhesion (CEACAM) molecules belong to a family of membrane glycoproteins that mediate intercellular interactions influencing cellular growth, immune cell activation, apoptosis, and tumor suppression. Several family members (CEACAM1, CEACAM5, and CEACAM6) are highly expressed in cancers, and they share a conserved N-terminal domain that serves as an attractive target for cancer immunotherapy. A multi-epitope vaccine candidate against this conserved domain has been developed using immunoinformatics tools. Specifically, several epitopes predicted to interact with MHC class I and II molecules were linked together with appropriate linkers. The tertiary structure of the vaccine is generated by homology and ab initio modeling. Molecular docking of epitopes to MHC structures have revealed that the lowest energy conformations are the epitopes bound to the antigen-binding groove of the MHC molecules. Subsequent molecular dynamics simulation has confirmed the stability of the binding conformations in solution. The predicted vaccine has relatively high antigenicity and low allergenicity, suggesting that it is an ideal candidate for further refinement and development.Communicated by Ramaswamy H. Sarma.
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