Literature DB >> 11422157

In vitro and in vivo responses to the recombinant bovine dander allergen Bos d 2 and its fragments.

P Ruoppi1, T Virtanen, T Zeiler, M Rytkönen-Nissinen, J Rautiainen, J Nuutinen, A Taivainen.   

Abstract

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.

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Year:  2001        PMID: 11422157     DOI: 10.1046/j.1365-2222.2001.01086.x

Source DB:  PubMed          Journal:  Clin Exp Allergy        ISSN: 0954-7894            Impact factor:   5.018


  3 in total

1.  Ablation of ovomucoid-induced allergic response by desensitization with recombinant ovomucoid third domain in a murine model.

Authors:  P Rupa; Y Mine
Journal:  Clin Exp Immunol       Date:  2006-09       Impact factor: 4.330

Review 2.  Addressing Molecular Diagnosis of Occupational Allergies.

Authors:  Monika Raulf; Santiago Quirce; Olivier Vandenplas
Journal:  Curr Allergy Asthma Rep       Date:  2018-02-14       Impact factor: 4.806

Review 3.  Recombinant allergen-based provocation testing.

Authors:  Verena Niederberger; Julia Eckl-Dorna; Gabrielle Pauli
Journal:  Methods       Date:  2013-08-03       Impact factor: 3.608

  3 in total

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