Receptor binding by cholera toxin B-subunit and amino acid modification improves minimal peptide immunogenecity
2012 (English)In: ISRN Molecular Biology, ISSN 2090-7907, Vol. 2012, 170676Article in journal (Refereed) Published
We increase our understanding of augmenting a cellular immune response, by using an HIV-1 protease-derived epitope (PR75−84), and variants thereof, coupled to the C-terminal, of the B subunit of cholera toxin (CTB). 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).
Place, publisher, year, edition, pages
Hindawi Publishing Corporation, 2012. Vol. 2012, 170676
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
IdentifiersURN: urn:nbn:se:liu:diva-84288DOI: 10.5402/2012/170676OAI: oai:DiVA.org:liu-84288DiVA: diva2:558499