In vitro and in vivo responses to the recombinant bovine dander allergen Bos d 2 and its fragments.
BACKGROUND
About one in every four cases of occupational rhinitis recorded in Finland is animal-induced. Bovine allergens are the most important in this respect and the largest patient group consists of dairy farmers. Allergen immunotherapy, if proven effective, safe and feasible, would be ideal for their treatment. The development of recombinant allergens has offered new potential therapeutic prospects. Fragments of recombinant Bos domesticus (Bos d 2) allergen could be suitable for this purpose because they are recognized by T cells but their IgE-binding capacity is attenuated.


OBJECTIVE
The aim of this study was to verify whether the potential of the two fragments of recombinant Bos d 2 (corresponding to amino acids 1-131 and 81-172) to induce immediate allergic reaction in a shock organ (nose) was decreased compared to the complete recombinant allergen, which would be an advantageous property for a preparation intended for allergen immunotherapy.


METHODS
The study group consisted of 10 dairy farmers with cow-induced allergic rhinitis. We used the IgE titres against native Bos d 2 measured by indirect IgE ELISA to characterize the level of sensitization and compared the IgE titres in the rhinitis patients with 12 cow-sensitized asthmatic farmers and 12 healthy students. In vitro reactivity against recombinant Bos d 2 and its two fragments was studied by indirect IgE ELISA and in vivo reactivity by nasal provocation tests.


RESULTS
The IgE titres against native Bos d 2 of patients with rhinitis tended to be lower than the titres of asthmatics. The healthy students did not exhibit any detectable IgE reactivity to native Bos d 2. In the patients with rhinitis, there was no statistically significant difference between IgE responses against native and recombinant Bos d 2, whereas with both in vitro and in vivo, the reactivity to both fragments of recombinant Bos d 2 was lower than the reactivity to the complete recombinant allergen.


CONCLUSIONS
Due to the decreased in vivo capacity to induce immediate allergic reactions, the fragments may be better tolerated in allergen immunotherapy than the complete allergen.
Ruoppi
P
P
Department of Otorhinolaryngology, Kuopio University Hospital, Kuopio, Finland.
Virtanen
T
T
Zeiler
T
T
Rytkönen-Nissinen
M
M
Rautiainen
J
J
Nuutinen
J
J
Taivainen
A
A
D000328:Adult; D000485:Allergens / Q000032:analysis*; D000818:Animals; D052179:Antigens, Plant; D002352:Carrier Proteins / Q000032:analysis*; D002417:Cattle; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D005387:Finland / Q000453:epidemiology; D006801:Humans; D007073:Immunoglobulin E / Q000032:analysis; D008297:Male; D008875:Middle Aged; D009299:Nasal Provocation Tests / Q000379:methods; D011994:Recombinant Proteins / Q000032:analysis; D012221:Rhinitis, Allergic, Perennial / Q000453:epidemiology / Q000276:immunology; D012882:Skin Tests; D018709:Statistics, Nonparametric
D000485:Allergens; D052179:Antigens, Plant; C113339:Bos d 2 allergen; D002352:Carrier Proteins; D011994:Recombinant Proteins; D007073:Immunoglobulin E