Correlating low-similarity peptide sequences and allergenic epitopes.
Although a high number of allergenic peptide epitopes has been experimentally identified and defined, the molecular basis and the precise mechanisms underlying peptide allergenicity are unknown. This issue was analyzed exploring the relationship between peptide allergenicity and sequence similarity to the human proteome. The structured analysis of the data reported in literature put into evidence that the most part of IgE-binding epitopes are (or harbor) pentapeptide unit(s) with no/low similarity to the human proteome, this way suggesting that no or low sequence similarity to the host proteome might represent a minimum common denominator identifying allergenic peptides. The present literature analysis might be of relevance in devising and designing short amino acid modules to be used for blocking pathogenic IgE.
Kanduc
D
D
Department of Biochemistry & Molecular Biology Ernesto Quagliariello, University of Bari, Italy. d.kanduc@biologia.uniba.it
D000485:Allergens / Q000009:adverse effects* / Q000276:immunology; D000595:Amino Acid Sequence; D000939:Epitopes / Q000276:immunology; D006801:Humans; D007073:Immunoglobulin E / Q000737:chemistry / Q000276:immunology / Q000378:metabolism; D010455:Peptides / Q000009:adverse effects* / Q000737:chemistry* / Q000276:immunology; D011485:Protein Binding / Q000276:immunology; D020543:Proteome / Q000276:immunology / Q000378:metabolism
D000485:Allergens; D000939:Epitopes; D010455:Peptides; D020543:Proteome; D007073:Immunoglobulin E