In vitro evaluation of digestive and endolysosomal enzymes to cleave CML‐modified Ara h 1 peptides. Issue 4 (12th March 2015)

• Record Type: Journal Article
• Authors: Mattison, Christopher P.; Dinter, Jens; Berberich, Matthew J.; Chung, Si‐Yin; Reed, Shawndrika S.; Le Gall, Sylvie; Grimm, Casey C.
• Is Part Of: Food science & nutrition. Volume 3:Issue 4(2015:Jul.)
• Page Start: 273
• Page End: 283
• Publication Date: 2015-03-12
• Subjects: Food industry and trade -- Periodicals; Food -- Periodicals; Nutrition -- Periodicals; 664
• DOI: 10.1002/fsn3.215
• Languages: English
• ISSNs: 2048-7177

Abstract

<abstract abstract-type="main" id="fsn3215-abs-0001"> <title>Abstract</title> <p>Ara h 1 is a major peanut allergen. Processing‐induced modifications may modulate the allergenic potency of Ara h 1. Carboxymethyl lysine (CML) modifications are a commonly described nonenzymatic modification on food proteins. In the current study, we tested the ability of digestive and endolysosomal proteases to cleave CML‐modified and unmodified Ara h 1 peptides. Mass spectrometric analyses of the digested peptides demonstrate that carboxymethylation of lysine residues renders these peptides refractory to trypsin digestion. We did not detect observable differences in the simulated gastric fluid or endolysosomal digestion between the parental and CML‐modified peptides. One of the tested peptides contains a lysine residue previously shown to be CML modified laying in a previously mapped linear IgE epitope, but we did not observe a difference in IgE binding between the modified and parental peptides. Our findings suggest a molecular mechanism for the increased resistance of peanut allergens modified by thermal processing, such as Ara h 1, to digestion in intestinal fluid after heating and could help explain how food processing‐induced modifications may lead to more potent food allergens by acting to protect intact IgE epitopes from digestion by proteases targeting lysine residues.</p> </abstract>