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Fusion proteins were used for immunizations of HLA-A0201 transgenic C57BL\/6 mice. We observed different capacities to elicit a cellular immune response by peptides with additions of five to ten amino acids to the PR epitope. There was a positive correlation between the magnitude of the elicited cellular immune response and the capacity of the fusion protein to bind GM-1. This binding capacity is affected by its ability to form natural pentamers of CTB. Our results suggest that functional CTB pentamers containing a foreign amino acid-modified epitope is a novel way to overcome the limited cellular immunogenicity of minimal peptide antigens. This way of using a functional assay as readout for improved cellular immunogenicity might become highly valuable for difficult immunogens such as short peptides (epitopes).<\/jats:p>","DOI":"10.5402\/2012\/170676","type":"journal-article","created":{"date-parts":[[2012,7,29]],"date-time":"2012-07-29T09:30:08Z","timestamp":1343554208000},"page":"1-9","source":"Crossref","is-referenced-by-count":0,"title":["Receptor Binding by Cholera Toxin B-Subunit and Amino Acid Modification Improves Minimal Peptide Immunogenicity"],"prefix":"10.5402","volume":"2012","author":[{"given":"Andreas","family":"Boberg","sequence":"first","affiliation":[{"name":"Department of Microbiology, Tumor and Cell Biology, Karolinska Institute, 171 82 Stockholm, Sweden"},{"name":"Division of Education and Research administration, M\u00e4lardalen University, P.O. 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