Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis
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...
| Published in: | Scientific Reports |
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| Main Authors: | , , , , , , , , |
| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-09-01
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| Online Access: | https://doi.org/10.1038/s41598-023-39599-0 |
| _version_ | 1850073435099627520 |
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| author | Kai Wang Judit Gali-Moya Maria Ruano-Zaragoza Kathleen Cain Giovanni D’Auria Matthew Daly Perdita Barran René Crevel E. N. Clare Mills |
| author_facet | Kai Wang Judit Gali-Moya Maria Ruano-Zaragoza Kathleen Cain Giovanni D’Auria Matthew Daly Perdita Barran René Crevel E. N. Clare Mills |
| author_sort | Kai Wang |
| collection | DOAJ |
| container_title | Scientific Reports |
| description | 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. |
| format | Article |
| id | doaj-art-c0e853e73666451a9ad1afbafaef4eae |
| institution | Directory of Open Access Journals |
| issn | 2045-2322 |
| language | English |
| publishDate | 2023-09-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| spelling | doaj-art-c0e853e73666451a9ad1afbafaef4eae2025-08-20T00:16:28ZengNature PortfolioScientific Reports2045-23222023-09-0113111110.1038/s41598-023-39599-0Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysisKai Wang0Judit Gali-Moya1Maria Ruano-Zaragoza2Kathleen Cain3Giovanni D’Auria4Matthew Daly5Perdita Barran6René Crevel7E. N. Clare Mills8School of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of BiotechnologySchool of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of BiotechnologyAllergy Department, Hospital Clinic of BarcelonaDepartment of Chemistry, Manchester Institute of BiotechnologyDepartment of Agricultural Sciences, University of Naples Federico IISchool of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of BiotechnologyDepartment of Chemistry, Manchester Institute of BiotechnologySchool of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of BiotechnologySchool of Biological Sciences, Manchester Academic Health Sciences Centre, Manchester Institute of BiotechnologyAbstract 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.https://doi.org/10.1038/s41598-023-39599-0 |
| spellingShingle | Kai Wang Judit Gali-Moya Maria Ruano-Zaragoza Kathleen Cain Giovanni D’Auria Matthew Daly Perdita Barran René Crevel E. N. Clare Mills Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis |
| title | Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis |
| title_full | Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis |
| title_fullStr | Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis |
| title_full_unstemmed | Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis |
| title_short | Bile salts enhance the susceptibility of the peach allergenic lipid transfer protein, Pru p 3, to in vitro gastrointestinal proteolysis |
| title_sort | bile salts enhance the susceptibility of the peach allergenic lipid transfer protein pru p 3 to in vitro gastrointestinal proteolysis |
| url | https://doi.org/10.1038/s41598-023-39599-0 |
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