IgE binding conformational epitopes of Asp f 3, a major allergen of Aspergillus fumigatus

Harikrishnan Ramachandran, Vasanthi Jayaraman, Banani Banerjee, Paul A. Greenberger, Kevin J. Kelly, Jordan N. Fink, Viswanath P. Kurup*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

26 Scopus citations


sp f 3 has been identified as one of the major allergens of Aspergillus fumigatus associated with the sensitization and immune responses in allergic bronchopulmonary aspergillosis (ABPA). In order to understand the structure/function relationship of Asp f 3, we studied synthetic peptides and constructed mutants deleted of specific IgE binding regions. The mutated allergens were obtained by expressing the genes and studied by ELISA for their reactivity with IgE from patients with ABPA. Seven linear IgE binding regions spanning the whole Asp f 3 molecule were demonstrated. The results demonstrated strong binding of IgE from ABPA patients with Asp f 3 and one mutant, Asp f 31-150, but not with other mutant constructs. The results identified 12 amino acids at the N-terminal end and 8 amino acids (143-150) at the C-terminal end as significant in the conformational constraints for IgE binding. The Fourier transfer spectra showed comparable β-sheet structure of Asp f 31-150 and Asp f 3, indicating the role of secondary structure in IgE binding. The primary and secondary structures may help understanding of the functional role the allergens play in the disease and may have implications in immunodiagnosis and probably immunotherapy.

Original languageEnglish (US)
Pages (from-to)324-333
Number of pages10
JournalClinical Immunology
Issue number3 I
StatePublished - 2002


  • Asp f 3
  • Aspergillus fumigatus
  • Deletion mutants
  • FTIR spectra
  • IgE epitopes
  • Molecular cloning
  • Synthetic peptides

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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