Peptide Immunogenicity

Structural and Thermodynamic Modeling of Peptide Immunogenicity

In the current paradigm of humoral immunity, the membrane-bound immunoglobulin (mIg) receptors of a particular B cell can recognize their cognate antigen through an epitope found on the native surface of the antigen. This recognition, along with co-activation by helper T cells, will stimulate the B cell to secrete anitbodies having the same antigen specificity as the mIg receptors. As such, the immunogenicity of native antigens, which are mostly proteins, is firmly established. It is interesting, therefore, to find examples in the literature wherein short peptide sequences from an antigenic protein are capable of inducing the production of antibodies both against the peptide and the corresponding region from the protein. The assumption taken here is that these peptides adopt stable structures that are also found in the native protein, even though typical linear peptides are inherently unstable due to their low folding stabilities.

Molecular Mimicry via Structural Homology of Cross-Reactive Peptides

Post-translational Modifications and Disorder-to-Order/Order-to-Disorder Structural Transitions