Faculty Collaboration Database

Immunodominant peptide epitopes of allergen, Asp f 1 from the fungus Aspergillus fumigatus. Peptides 1998;19(9):1469-77

Date

12/24/1998

Pubmed ID

9864052

DOI

10.1016/s0196-9781(98)00113-2

Scopus ID

2-s2.0-0032439815 (requires institutional sign-in at Scopus site)   41 Citations

Abstract

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.

Author List

Kurup VP, Banerjee B, Murali PS, Greenberger PA, Krishnan M, Hari V, Fink JN

MESH terms used to index this publication - Major topics in bold

Allergens
Amino Acid Sequence
Antigens, Plant
Aspergillus fumigatus
B-Lymphocytes
Fungal Proteins
Humans
Immunodominant Epitopes
Immunoglobulin E
Lymphocyte Activation
Molecular Sequence Data
Oligopeptides
Protein Binding
Ribonucleases
T-Lymphocytes