IgE Binding Conformational Epitopes of Asp f 3, a Major Allergen of Aspergillus fumigatus

2002 ◽  
Vol 103 (3) ◽  
pp. 324-333 ◽  
Author(s):  
Harikrishnan Ramachandran ◽  
Vasanthi Jayaraman ◽  
Banani Banerjee ◽  
Paul A. Greenberger ◽  
Kevin J. Kelly ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Major Allergen ◽  
Ige Binding ◽  
Conformational Epitopes

scholarly journals Immunological Characterization of Asp f 2, a Major Allergen from Aspergillus fumigatus Associated with Allergic Bronchopulmonary Aspergillosis

1998 ◽  
Vol 66 (11) ◽  
pp. 5175-5182 ◽  
Author(s):  
Banani Banerjee ◽  
Paul A. Greenberger ◽  
Jordan N. Fink ◽  
Viswanath P. Kurup
Keyword(s):  
Aspergillus Fumigatus ◽  
Matrix Protein ◽  
Expression System ◽  
Allergic Bronchopulmonary Aspergillosis ◽  
Major Allergen ◽  
Extracellular Matrix Protein ◽  
Fungal Culture ◽  
Homologous Proteins ◽  
Ige Binding ◽  
Prokaryotic Expression System

ABSTRACT The 37-kDa recombinant protein Asp f 2, encoding an allergen ofAspergillus fumigatus, was expressed in a prokaryotic expression system and immunologically evaluated for its functional and structural properties. The open reading frame for a 310-amino-acid-long protein was shown to encode a signal peptide of 31 amino acids. A native 37-kDa culture filtrate protein and a 55-kDa mycelial glycoprotein (gp55) exhibited complete N-terminal sequence homology to Asp f 2. A GenBank search for homologous proteins revealed 60 and 44% sequence homologies to the cytosolic protein ASPND1 fromAspergillus nidulans and fibrinogen binding protein fromCandida albicans, respectively. The glycosylation sites and cysteine molecules are conserved in all the three proteins. The extracellular matrix protein laminin showed a dose-dependent interaction with Asp f 2. This protein, expressed as a major cell-associated protein within 24 h of in vitro fungal culture, comprises 20 to 40% of total fungal protein. Furthermore, both native and recombinant Asp f 2 exhibited specific immunoglobulin (IgE) binding with allergic bronchopulmonary aspergillosis (ABPA) and cystic fibrosis-ABPA patients, whereas A. fumigatus-sensitized allergic asthma and normal control subjects failed to show IgE binding with Asp f 2. These results indicate that Asp f 2 is a major allergen of A. fumigatus exhibiting IgE antibody binding with sera from patients with ABPA. The antigen should be explored further for its potential role in the differential diagnosis of A. fumigatus-associated allergic diseases.

ENEA, a peach and apricot IgE-binding protein cross-reacting with the latex major allergen Hev b 5

2019 ◽  
Vol 112 ◽  
pp. 347-357 ◽  
Author(s):  
Ivana Giangrieco ◽  
Teresa Ricciardi ◽  
Claudia Alessandri ◽  
Lucia Farina ◽  
Roberta Crescenzo ◽  
...  
Keyword(s):  
Binding Protein ◽  
Major Allergen ◽  
Ige Binding

Mapping and Mutational Analysis of the IgE-Binding Epitopes on Ara h 1, a Legume Vicilin Protein and a Major Allergen in Peanut Hypersensitivity

1997 ◽  
Vol 245 (2) ◽  
pp. 334-339 ◽  
Author(s):  
A. Wesley Burks ◽  
David Shin ◽  
Gael Cockrell ◽  
J. Steven Stanley ◽  
Ricki M. Helm ◽  
...  
Keyword(s):  
Mutational Analysis ◽  
Major Allergen ◽  
Ige Binding ◽  
Ara H 1

Isolation and Characterization of a Relevant Aspergillus fumigatus Antigen with IgG- and IgE-Binding Activity

1988 ◽  
Vol 86 (2) ◽  
pp. 176-182 ◽  
Author(s):  
Viswanath P. Kurup ◽  
Muthiah Ramasamy ◽  
Paul A. Greenberger ◽  
Jordan N. Fink
Keyword(s):  
Aspergillus Fumigatus ◽  
Binding Activity ◽  
Isolation And Characterization ◽  
Ige Binding

Narrow Leafed Lupin Beta-Conglutin Proteins Epitopes Identification and Molecular Features Analysis Involved in Cross-Allergenicity to Peanut and Other Legumes

2016 ◽  
Vol 2 (1) ◽  
pp. 29 ◽  
Author(s):  
Elena Lima-Cabello ◽  
Paula Robles-Bolivar ◽  
Juan D. Alché ◽  
Jose C. Jimenez-Lopez
Keyword(s):  
In Silico Analysis ◽  
Major Allergen ◽  
T Cell Epitopes ◽  
Structural Elements ◽  
New Family ◽  
Molecular Features ◽  
Ige Binding ◽  
Ara H 1 ◽  
Differential Variability ◽  
Silico Analysis

The use of narrow leafed lupin - NLL (Lupinus angustifolius L.) as a new food is resulting in an increasing number of allergic reactions cases, particularly in atopic patients with other pre-existing legume allergies. In the current study, we have performed an extensive in silico analysis of the NLL seed β-conglutin proteins, a new family of major allergen proteins identified in NLL, and a comparison to other relevant food allergens such as peanut Ara h 1. We analysed the variability of surface residues involved in conformational IgE-binding epitopes, lineal B- and T-cell epitopes, and changes in 2-D structural elements and 3D motives, with the aim to investigate cross-allergenicity among lupin, peanut, and other different legumes. Our results revealed that considerable structural differences exist, particularly affecting 2-D elements (loops and coils), and numerous micro-heterogeneities are present in fundamental residues directly involved in epitopes differential variability. Thus, variability of residues involved in IgE-binding epitopes might be a major contributor to the observed differences in cross-allergenicity among legumes.

The IgE-binding epitopes of rPar j 2, a major allergen ofParietaria judaicapollen, are heterogeneously recognized among allergic subjects

Allergy ◽  
2000 ◽  
Vol 55 (3) ◽  
pp. 246-250 ◽  
Author(s):  
M. Assunta Costa ◽  
G. Duro ◽  
V. Izzo ◽  
P. Colombo ◽  
M. G. Mirisola ◽  
...  
Keyword(s):  
Major Allergen ◽  
Ige Binding

The IgE-Binding Regions of the Major Allergen Pen a 1: Multiple Epitopes or Intramolecular Cross-Reactivity?

2001 ◽  
Vol 124 (1-3) ◽  
pp. 103-106 ◽  
Author(s):  
G. Reese ◽  
R. Ayuso ◽  
S.M. Leong-Kee ◽  
M. Plante ◽  
S.B. Lehrer
Keyword(s):  
Major Allergen ◽  
Cross Reactivity ◽  
Ige Binding ◽  
Binding Regions ◽  
Pen A 1

scholarly journals Use of a Synthetic Peptide Epitope of Asp f 1, a Major Allergen or Antigen of Aspergillus fumigatus, for Improved Immunodiagnosis of Allergic Bronchopulmonary Aspergillosis

2004 ◽  
Vol 11 (3) ◽  
pp. 552-558 ◽  
Author(s):  
Taruna Madan ◽  
Priyanka Priyadarsiny ◽  
Mudit Vaid ◽  
Neel Kamal ◽  
Ashok Shah ◽  
...  
Keyword(s):  
Aspergillus Fumigatus ◽  
Synthetic Peptide ◽  
Immunoglobulin E ◽  
Allergic Bronchopulmonary Aspergillosis ◽  
Major Allergen ◽  
Specific Ige ◽  
Diagnostic Efficiency ◽  
Intradermal Testing ◽  
Peptide Epitope ◽  
Asp F 1

ABSTRACT Allergic bronchopulmonary aspergillosis (ABPA) is an immunologically complex allergic disorder caused by the fungal pathogen Aspergillus fumigatus. Elevated levels of total immunoglobulin E (IgE), specific IgE, and IgG antibodies in sera are important immunodiagnostic criteria for ABPA. International reference standards or standardized immunodiagnostic assays are not available due to a lack of well-defined diagnostic antigens. The present study was carried out to identify and evaluate the immunodiagnostic relevance of synthetic epitopic peptides of Asp f 1, a major allergen, antigen, or cytotoxin of A. fumigatus. Five overlapping peptides were synthesized from the N terminus of Asp f 1, one of the potential immunodominant regions predicted by algorithmic programs. The 11-amino-acid synthetic peptide (P1) significantly inhibited both IgG binding (89.10% ± 4.45%) and IgE binding (77.32% ± 3.38%) of the standardized diagnostic antigen (SDA) (a well-defined pool of diagnostically relevant allergens and antigens of A. fumigatus). With a panel of sera of ABPA patients, allergic patients with skin test negativity to A. fumigatus, and healthy individuals, P1 showed a higher diagnostic efficiency than SDA (specific IgG, 100%; specific IgE, 98.3%). The diagnostic efficiency of P1 could be attributed to the presence of homologous epitopes in various immunodominant allergens or antigens of A. fumigatus. The ability of P1 to induce histamine release from sensitized mast cells and a Th2 type of cytokine profile in peripheral blood mononuclear cells of ABPA patients suggests its potential for use in intradermal testing. P1 could be further explored for development of a standardized, specific, and sensitive immunodiagnostic test for aspergillosis.

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