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Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis.
Wang, Kai; Gali-Moya, Judit; Ruano-Zaragoza, Maria; Cain, Kathleen; D'Auria, Giovanni; Daly, Matthew; Barran, Perdita; Crevel, René; Mills, E N Clare.
Afiliación
  • Wang K; School of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
  • Gali-Moya J; School of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
  • Ruano-Zaragoza M; Allergy Department, Hospital Clinic of Barcelona, 08036, Barcelona, Spain.
  • Cain K; Department of Chemistry, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
  • D'Auria G; Department of Agricultural Sciences, University of Naples Federico II, Portici, Italy.
  • Daly M; School of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
  • Barran P; Department of Chemistry, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
  • Crevel R; School of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
  • Mills ENC; René Crevel Consulting Ltd, Suite A 82 James Carter Road, Mildenhall, IP28 7HP, UK.
Sci Rep ; 13(1): 15155, 2023 09 13.
Article en En | MEDLINE | ID: mdl-37704681
ABSTRACT
Sensitisation to the lipid transfer protein Pru p 3 is associated with severe allergic reactions to peach, the proteins stability being thought to play a role in its allergenicity. Lipid binding increases susceptibility of Pru p 3 to digestion and so the impact of bile salts on the in vitro gastrointestinal digestibility of Pru p 3 was investigated and digestion products mapped by SDS-PAGE and mass spectrometry. Bile salts enhanced the digestibility of Pru p 3 resulting in an ensemble of around 100 peptides spanning the protein's sequence which were linked by disulphide bonds into structures of ~ 5-6 kDa. IgE binding studies with a serum panel from peach allergic subjects showed digestion reduced, but did not abolish, the IgE reactivity of Pru p 3. These data show the importance of including bile salts in vitro digestion systems and emphasise the need to profile of digestion in a manner that allows identification of immunologically relevant disulphide-linked peptide aggregates.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos / Prunus persica Límite: Humans Idioma: En Revista: Sci Rep Año: 2023 Tipo del documento: Article País de afiliación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alérgenos / Prunus persica Límite: Humans Idioma: En Revista: Sci Rep Año: 2023 Tipo del documento: Article País de afiliación: Reino Unido