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Infection and Immunity, May 1999, p. 2284-2291, Vol. 67, No. 5
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Conformational and Linear B-Cell Epitopes of Asp f 2, a Major Allergen of Aspergillus fumigatus, Bind Differently to Immunoglobulin E Antibody in the Sera of Allergic Bronchopulmonary Aspergillosis Patients

Banani Banerjee,1 Paul A. Greenberger,2 Jordan N. Fink,1 and Viswanath P. Kurup1,*

Department of Medicine, Allergy-Immunology Division, Medical College of Wisconsin, Milwaukee, Wisconsin 53226, and Research Service, Veterans Affairs Medical Center, Milwaukee, Wisconsin 53295,1 and Division of Allergy-Immunology, Northwestern University Medical School, Chicago, Illinois 606112

Received 11 January 1999/Returned for modification 29 January 1999/Accepted 11 February 1999

Asp f 2 is a major Aspergillus fumigatus allergen involved in allergic bronchopulmonary aspergillosis. Knowledge of the B-cell epitopes may contribute to the understanding of immunoregulation and immunodiagnosis. To elucidate the immunoglobulin E (IgE) binding epitopes in the linear sequence of Asp f 2, we synthesized decamer peptides spanning the whole molecule of Asp f 2 on derivatized cellulose membranes and evaluated IgE binding in ABPA patient and control sera. Peptides three to five amino acids long were synthesized based on amino acid sequences within the IgE binding regions and evaluated for the specificity of epitope antibody interactions. Nine IgE binding regions were recognized in this protein of 268 amino acid residues. Of the nine epitopes, seven (ATQRRQI, RKYFG, HWR, YTTRR, DHFAD, ALEAYA, and THEGGQ) are present in the hydrophilic regions of Asp f 2. Immunologic evaluation of the three recombinant fragments, Asp f 2A encompassing the N-terminal epitope region, Asp f 2B without N- and C-terminal regions of the protein, and Asp f 2C representing C-terminal epitopes, revealed that either the N- or C-terminal region of the protein is essential for the correct folding and conformation for IgE antibody binding.

* Corresponding author. Mailing address: VA Medical Center, Research Service 151-I, 5000 West National Ave., Milwaukee, WI 53295. Phone: (414) 384-2000, ext. 1459 or 1510. Fax: (414) 382-5374. E-mail: vkurup{at}post.its.mcw.edu.

Infection and Immunity, May 1999, p. 2284-2291, Vol. 67, No. 5
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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