Antibody binding of deletion mutants of Asp f 2, the major Aspergillus fumigatus allergen

Bin Tang*, Banani Banerjee, Paul A. Greenberger, Jordan N. Fink, Kevin J. Kelly, Viswanath P. Kurup

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

24 Scopus citations


Asp f 2, a 268 amino acid major allergen from Aspergillus fumigatus (Af) demonstrated nine linear IgE binding regions. It is not known whether any of these linear epitopes are also conformatory epitopes. Hence, we constructed deletion mutants of Asp f 2 devoid of one or more epitopes, and the IgE binding of these proteins with sera from patients with ABPA was compared with the full-length Asp f 2 expressed in E. coli and Pichia. The Pichia expressed protein reacted weakly with IgE, but strongly with IgG of ABPA sera compared to E. coli expressed Asp f 2. Weak IgE binding only was seen when the C-terminal or N-terminal was deleted, while depletion of both ends negated all reactivity. The monoclonal antibody IL-B8 and IgE and IgG of ABPA sera bound significantly to the Asp f 2 E-4 fragment indicating that the major B-cell epitope is located at the N-terminal end of Asp f 2. (C) 2000 Academic Press.

Original languageEnglish (US)
Pages (from-to)1128-1135
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - Apr 21 2000


  • Asp f 2
  • Aspergillus fumigatus
  • Deletion mutants
  • IgE
  • Immune response

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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