Immunodominant peptide epitopes of allergen, Asp f 1 from the fungus Aspergillus fumigatus

Viswanath P. Kurup*, B. Banerjee, P. S. Murali, P. A. Greenberger, M. Krishnan, V. Hari, J. N. Fink

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

40 Scopus citations


Aspergillus fumigatus ribotoxin Asp f 1 is a major allergen with IgE binding activity to serum of a majority of patients with allergic bronchopulmonary aspergillosis (ABPA). The IgE binding epitopes or the T- cell stimulatory peptides of this molecule have not been studied. In the present investigation, we have synthesized linear decapeptides spanning the whole molecule of Asp f 1 and analyzed their IgE binding properties. We have also synthesized peptides based on their possible T-cell stimulatory properties and studied the stimulation of peripheral blood mononuclear cells from ABPA patients and normal controls. Several peptides demonstrated distinct IgE antibody binding response against sera from ABPA patients and proliferative response against peripheral blood mononuclear cells from the patients. From the results, it can be concluded that the carboxy-terminal region of Asp f 1 representing amino acid residues 115-149 involved in both humoral and cell mediated immunoresponses in ABPA.

Original languageEnglish (US)
Pages (from-to)1469-1477
Number of pages9
Issue number9
StatePublished - 1998


  • Allergic bronchopulmonary aspergillosis
  • Aspergillus fumigatus
  • B-cell epitope T-cell epitope

ASJC Scopus subject areas

  • Endocrinology
  • Cellular and Molecular Neuroscience
  • Biochemistry
  • Physiology


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