IgE reactivity to profilin in pollen-sensitized subjects with adverse reactions to banana and pineapple.
BACKGROUND
The so-called 'latex-fruit syndrome' is a well-documented phenomenon in cross-reactive allergies. By contrast, there is a lack of information about allergy to exotic fruits in patients with a predominant pollen sensitization. Since the ubiquitous protein profilin has been identified as an allergen in natural rubber latex as well as in pollen-related foods, the aim of this study was to investigate the role of profilin in allergy to certain exotic fruits.


METHODS
Recombinant profilins from banana and pineapple were cloned by a PCR technique after isolation of total RNA using degenerated profilin-specific primers. The unknown 5' ends of copy DNA (cDNA) were identified by rapid amplification of 5'cDNA ends (5'-RACE) and expression in Escherichia coli BL21(DE3) cells. The recombinant profilins were purified by affinity chromatography using poly-(L)-proline as the solid phase. IgE-binding capabilities were characterized by means of immunoblot and Enzyme Allergosorbent Test (EAST). The cross-reactivity to birch pollen profilin and latex profilin was studied by EAST as well as by immunoblot inhibition experiments.


RESULTS
Both banana and pineapple profilin were found to consist of 131 amino acid residues with high amino acid sequence identity to known allergenic pollen and food profilins (71-84%). IgE binding to the recombinant profilins was observed in 7/16 sera from subjects with suspected banana allergy (44%) and in 8/19 sera from subjects with suspected pineapple allergy (42%). Inhibition experiments indicated similar IgE reactivity of natural and recombinant allergens. In addition, high cross-reactivity to birch pollen profilin Bet v 2 and latex profilin Hev b 8 was demonstrated by immunoblot inhibition as well as EAST inhibition experiments.


CONCLUSIONS
Since a high IgE-binding prevalence of about 40% was obtained in both banana and pineapple allergy, we conclude that profilin is an important mediator of IgE cross-reactivity between pollen and exotic fruits.
Reindl
J
J
Department of Allergology, Paul-Ehrlich-Institut, Langen, Germany.
Rihs
H P
HP
Scheurer
S
S
Wangorsch
A
A
Haustein
D
D
Vieths
S
S
D000328:Adult; D000485:Allergens / Q000009:adverse effects / Q000276:immunology / Q000378:metabolism; D000918:Antibody Specificity; D015153:Blotting, Western; D003285:Contractile Proteins; D003429:Cross Reactions / Q000276:immunology; D005260:Female; D005512:Food Hypersensitivity / Q000097:blood / Q000209:etiology / Q000276:immunology*; D005638:Fruit / Q000009:adverse effects*; D006801:Humans; D007073:Immunoglobulin E / Q000097:blood / Q000276:immunology*; D020315:Latex Hypersensitivity / Q000276:immunology; D008297:Male; D008840:Microfilament Proteins / Q000009:adverse effects / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D008875:Middle Aged; D010940:Plant Proteins / Q000009:adverse effects / Q000276:immunology* / Q000378:metabolism; D011058:Pollen / Q000009:adverse effects / Q000276:immunology; D051304:Profilins; D011485:Protein Binding; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000276:immunology; D020133:Reverse Transcriptase Polymerase Chain Reaction
D000485:Allergens; D003285:Contractile Proteins; D008840:Microfilament Proteins; D010940:Plant Proteins; D051304:Profilins; D011994:Recombinant Proteins; D007073:Immunoglobulin E