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Assessment of IgE and IgG4 Binding Capacities of Cow's Milk Proteins Selectively Altered by Proteases.

Authors
  • Charcosset, Alexandre1
  • Adel-Patient, Karine1
  • Dupont, Christophe2
  • Bernard, Hervé1
  • 1 UMR Service de Pharmacologie et d'Immunoanalyse, CEA-INRA, Université Paris-Saclay , CEA de Saclay, F-91191 Gif-sur-Yvette, France. , (France)
  • 2 Pediatric Gastroenterology Service, Hôpital Necker Enfants Malades , F-75015 Paris, France. , (France)
Type
Published Article
Journal
Journal of Agricultural and Food Chemistry
Publisher
American Chemical Society
Publication Date
May 04, 2016
Volume
64
Issue
17
Pages
3394–3404
Identifiers
DOI: 10.1021/acs.jafc.5b01782
PMID: 27015440
Source
Medline
Keywords
License
Unknown

Abstract

Specific IgE and IgG4 have been reported to play key roles in the context of IgE-mediated cow's milk allergy (CMA), but the persistence of their epitopes in milk hydrolysates has not been evaluated. Using sera from 32 CMA patients, 6 CMA patients treated by epicutaneous therapy (CM-treated), and 4 CM-tolerant peanut allergic patients, we analyzed the IgE and IgG4 binding capacities related to major milk allergens in processed milk. Different proteases (plasmin, chymosin, α-chymotrypsin, or pepsin) were used progressively and selectively to hydrolyze β-lactoglobulin (β-LG) and casein (CN) in milk. We then showed that proteases differentially affect IgE or IgG4 immunoreactivities of CN and β-LG and also that we could not relate IgE and/or IgG4 levels or specificities to milk hydrolysates to the clinical status of the patients.

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