Conversion of orally induced suppression of the mucosal immune response to ovalbumin into stimulation by conjugating ovalbumin to cholera toxin or its B subunit

Vaccine ◽  
1994 ◽  
Vol 12 (6) ◽  
pp. 521-526 ◽  
Author(s):  
W STOK ◽  
P VANDERHEIJDEN ◽  
A BIANCHI
Keyword(s):  
Immune Response ◽  
Cholera Toxin ◽  
Mucosal Immune Response ◽  
B Subunit

scholarly journals Receptor Binding by Cholera Toxin B-Subunit and Amino Acid Modification Improves Minimal Peptide Immunogenicity

2012 ◽  
Vol 2012 ◽  
pp. 1-9
Author(s):  
Andreas Boberg ◽  
Alexandra Stålnacke ◽  
Andreas Bråve ◽  
Jorma Hinkula ◽  
Britta Wahren ◽  
...  
Keyword(s):  
Immune Response ◽  
Amino Acid ◽  
Cholera Toxin ◽  
Cellular Immune Response ◽  
Binding Capacity ◽  
Functional Assay ◽  
Cholera Toxin B Subunit ◽  
Acid Modification ◽  
B Subunit ◽  
Cellular Immune

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).

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