T-cell epitopes of the major peach allergen, Pru p 3: Identification and differential T-cell response of peach-allergic and non-allergic subjects.
Lipid transfer proteins (LTPs), particularly peach Pru p 3, are the most relevant plant food allergens in the South of Europe, and, therefore, their allergic properties have been extensively studied. However, neither T-cell epitopes nor their effect on the patients' T-cell response has been investigated in any member of the LTP panallergen family. The objective of the present study was to map the major T-cell epitopes of Pru p 3, as well as to evaluate their induced T-cell response in peach-allergic versus control subjects. Thus, peripheral blood mononuclear cells (PBMCs) from 18 peach-allergic patients and Pru p 3-specific T-cell lines (TCLs) from 9 of them were cultured with Pru p 3 and with a panel of 17 derived peptides (10-mer overlapping in 5 amino acids representing the full sequence of Pru p 3). Proliferation in 5-day assays was carried out via tritiated-thymidine incorporation, while IL4 and IFNgamma production was assessed via sandwich enzyme-linked immunosorbent tests (ELISA) of TCL culture supernatants. The results were compared to those obtained from 10 non-peach allergic control volunteers. Two consecutive peptides showed the highest activation capacity. About 74% of PBMCs and TCLs recognized them, forming a single T-epitope: Pru p 3(65-80). Additionally, other specific T-cell epitopes were observed. Pru p 3(25-35) was detected by more than 60% of TCLs from peach-allergic patients, and Pru p 3(45-55) only activated PBMCs from control subjects. Interestingly, TCLs from patients were associated with a Th2-type, whereas control TCLs presented a Th1-type cytokine response. The major immunogenic T-cell epitope identified in Pru p 3, Pru p 3(65-80), is a good candidate to develop new vaccines for hypersensitivity reactions associated with LTP allergens from Rosaceae fruits.
Tordesillas
Leticia
L
Unidad de Bioquimica, Departamento de Biotecnologia, E.T.S. Ingenieros Agronomos, UPM, Madrid, Spain.
Cuesta-Herranz
Javier
J
Gonzalez-Muñoz
Miguel
M
Pacios
Luis F
LF
Compés
Esther
E
Garcia-Carrasco
Belen
B
Sanchez-Monge
Rosa
R
Salcedo
Gabriel
G
Diaz-Perales
Araceli
A
D000485:Allergens / Q000737:chemistry / Q000276:immunology*; D000595:Amino Acid Sequence; D052179:Antigens, Plant / Q000276:immunology* / Q000378:metabolism; D018604:Epitope Mapping; D018984:Epitopes, T-Lymphocyte / Q000276:immunology* / Q000378:metabolism; D005512:Food Hypersensitivity / Q000276:immunology* / Q000378:metabolism; D006801:Humans; D007371:Interferon-gamma / Q000096:biosynthesis / Q000276:immunology; D015847:Interleukin-4 / Q000096:biosynthesis / Q000276:immunology; D008969:Molecular Sequence Data; D010455:Peptides / Q000276:immunology / Q000378:metabolism; D010940:Plant Proteins; D011487:Protein Conformation; D027861:Prunus / Q000276:immunology* / Q000378:metabolism; D014612:Vaccines / Q000737:chemistry / Q000276:immunology
D000485:Allergens; D052179:Antigens, Plant; D018984:Epitopes, T-Lymphocyte; C508598:IL4 protein, human; D010455:Peptides; D010940:Plant Proteins; C463181:Pru p 3 allergen; D014612:Vaccines; D015847:Interleukin-4; D007371:Interferon-gamma