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Immunochemical characterization of edible bird's nest allergens
1Department of Paediatrics, National University of Singapore, 5 Lower Kent Ridge Road, S(119074)Singapore.
Background:
We have previously described anaphylaxis induced by edible bird's nest (BN) and demonstrated that this condition is IgE mediated.
Objectives:
This study aimed at describing the immunochemical properties of the BN allergens. Comparative studies between 3 commercially available sources (according to the country of origin) of BN were also made.
Methods:
Crude extracts of commercially available processed BN from Sarawak (Malaysia), Thailand, and Indonesia and fresh unprocessed BN from the caves of Sarawak were obtained by means of aqueous extraction. Specific IgE toward these sources were determined by using fluorescence allergosorbent tests (FASTs). Cross-reactivity studies between the 3 sources of commercially available processed BN were carried out by means of FAST inhibition. Immunochemical characterization by means of IgE immunoblot, periodate treatment, and heat stability studies were carried out on fresh unprocessed BN from Sarawak.
Results:
Serum from allergic patients showed differences in IgE binding to the 3 sources of commercially available BN, with the highest levels of specific IgE recorded with the Sarawak source (P <.0001). Of these, only the Sarawak and Thailand sources showed considerable cross-reactivity. Further work on the unprocessed fresh Sarawak source identified a putative 66-kd major allergen containing several isoforms. Periodate treatment resulted in loss of IgE binding. Despite a progressive decline in the molecular weights of allergens on SDS-PAGE with increasing periods of boiling, IgE binding, as assessed by means of FAST, was not affected. N-terminal sequence of the major putative allergen (66 kd) showed homology to a domain of an ovoinhibitor precursor in chicken (SWISS-PROT accession No. P10184).
Conclusions:
We have described the immunochemical properties of BN allergens. Edible BN from different sources are allergenically dissimilar. The putative major allergen is a 66-kd protein.
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