Lipid-transfer proteins as potential plant panallergens: cross-reactivity among proteins of Artemisia pollen, Castanea nut and Rosaceae fruits, with different IgE-binding capacities.
BACKGROUND
Lipid-transfer proteins (LTPs), but not Bet v 1 homologues, have been identified as major allergens of apple and peach in the Rosaceae fruit-allergic population in the Mediterranean area. Many of these patients show cosensitization to mugwort pollen. LTPs have an ubiquitous distribution in tissues of many plant species, and have been proposed as a novel type of plant panallergens.


OBJECTIVE
We sought to isolate LTPs from Artemisia pollen and from a plant food not belonging to the Rosaceae family, such as chestnut nut, and to compare their amino acid sequences and IgE-binding capacities with those of apple and peach LTPs.


METHODS
Allergens (LTPs) were isolated by different chromatographic methods (gel-filtration, ion exchange and/or reverse-phase HPLC), and characterized by N-terminal amino acid sequencing and MALDI analysis. Specific IgE-quantification and immunodetection, as well as immunoblot and ELISA inhibition assays, were carried out using sera from patients allergic to both apple and peach.


RESULTS
Purified LTPs from Artemisia pollen and from chestnut seed showed molecular masses about 9 700d, and 43-50% sequence identity with the equivalent allergens of apple and peach in the first 30 N-terminal residues, which comprise about one third of the total amino acid sequence. A similar degree of sequence identity (50%) was found between the Artemisia and chestnut proteins. Both isolated LTPs bound specific IgE of sera from Rosaceae fruits allergic patients. However, substantially lower values of specific IgE-binding and maximum ELISA inhibition percentages were obtained for Artemisia and chestnut LTPs when compared to those from apple and peach.


CONCLUSIONS
LTPs from Artemisia pollen and chestnut crossreact with allergens (LTPs) of Rosaceae fruits, but significant differences in specific IgE-binding capacities were observed among members of the plant LTP family. Thus, further studies are needed to evaluate the clinical significance of the observed cross-reactivities of plant LTPs.
Díaz-Perales
A
A
Unidad de Bioquímica, Departamento de Biotecnología, Ingenieros Agrónomos, ALK-Abelló, Madrid, Spain.
Lombardero
M
M
Sánchez-Monge
R
R
García-Selles
F J
FJ
Pernas
M
M
Fernández-Rivas
M
M
Barber
D
D
Salcedo
G
G
D000485:Allergens / Q000032:analysis* / Q000276:immunology; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D005638:Fruit / Q000276:immunology*; D007073:Immunoglobulin E / Q000276:immunology*; D008969:Molecular Sequence Data; D009754:Nuts / Q000276:immunology*; D010940:Plant Proteins / Q000032:analysis* / Q000276:immunology; D011058:Pollen / Q000276:immunology*
D000485:Allergens; D010940:Plant Proteins; D007073:Immunoglobulin E