Conformational stability of digestion-resistant peptides of peanut conglutins reveals the molecular basis of their allergenicity
نویسندگان
چکیده
Conglutins represent the major peanut allergens and are renowned for their resistance to gastro-intestinal digestion. Our aim was to characterize the digestion-resistant peptides (DRPs) of conglutins by biochemical and biophysical methods followed by a molecular dynamics simulation in order to better understand the molecular basis of food protein allergenicity. We have mapped proteolysis sites at the N- and C-termini and at a limited internal segment, while other potential proteolysis sites remained unaffected. Molecular dynamics simulation showed that proteolysis only occurred in the vibrant regions of the proteins. DRPs appeared to be conformationally stable as intact conglutins. Also, the overall secondary structure and IgE-binding potency of DRPs was comparable to that of intact conglutins. The stability of conglutins toward gastro-intestinal digestion, combined with the conformational stability of the resulting DRPs provide conditions for optimal exposure to the intestinal immune system, providing an explanation for the extraordinary allergenicity of peanut conglutins.
منابع مشابه
Immunoglobulin E cross-reactivity between lupine conglutins and peanut allergens in serum of lupine-allergic individuals.
BACKGROUND Lupine is used increasingly in food products. The development of lupine allergy in peanut-allergic patients is believed to occur as a result of cross-reactivity between lupine and peanut proteins. OBJECTIVE To investigate the degree of immunoglobulin (Ig) E cross-reactivity between allergens in lupine and peanut. METHODS We investigated IgE cross-reactivity between lupine alpha-,...
متن کاملProtein Stability, Folding, Disaggregation and Etiology of Conformational Malfunctions
Estimation of protein stability is important for many reasons: first providing an understanding of the basic thermodynamics of the process of folding, protein engineering, and protein stability plays important role in biotechnology especially in food and protein drug design. Today, proteins are used in many branches, including industrial processes, pharmaceutical industry, and medical fields. A...
متن کاملStructure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation.
In the past decade, there has been an increase in allergic reactions to peanut proteins, sometimes resulting in fatal anaphylaxis. The development of improved methods for diagnosis and treatment of peanut allergies requires a better understanding of the structure of the allergens. Ara h 1, a major peanut allergen belonging to the vicilin family of seed storage proteins, is recognized by serum I...
متن کاملProbing Conformational Feature of a Recombinant Pyruvate Kinase by Limited Proteolysis
Pyruvate kinase is a key enzyme in glycolytic pathway that catalyzes the transphosphorylation between phosphoenolpyruvate and ADP to yield ATP and Pyruvate. Geobacillus stearothermophillus has a stable pyruvate kinase with determined crystal structure that composed of four separate domains. Given that limited proteolysis experiments can be successfully used to probe conformational features of p...
متن کاملLegumes, Nuts, and Seeds: Allergen Stability and Allergenicity of Processed Foods
Most severe allergic reactions, including fatal events, after ingestion of peanuts, soybeans and tree nuts have been reported. Allergens from legumes, nuts, and seeds are predominantly highly potent and stable to food processing. However, it is possible to alter the allergenicity potentially by various procedures. Heat treatments (dry heating, roasting, or baking) and enzymatic digestion affect...
متن کامل