Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies

Chow, Lu-Ping; LIU, Shu-Ling; Yu, Chih-Sheng; LIAO, Hsin-Kai; Tsai, Jaw‐Ji; TANG, Tswen-Kei

doi:10.1042/0264-6021:3460423

Cited by 18 publications

(13 citation statements)

References 23 publications

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“…4c–f). In contrast, the epitope sequences of the peanut allergen Ara h 1 (Schein et al, 2005) and the fungal allergen Asp f 13 (Chow et al, 2000)map to various areas of the protein (Fig. 5).…”

Section: Resultsmentioning

confidence: 99%

Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes

Oezguen

Zhou

Negi

et al. 2008

Molecular Immunology

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Similarities in sequences and 3D structures of allergenic proteins provide vital clues to identify clinically relevant IgE cross-reactivities. However, experimental 3D structures are available in the Protein Data Bank for only 5% (45/829) of all allergens catalogued in the Structural Database of Allergenic Proteins (SDAP, http://fermi.utmb.edu/SDAP). Here, an automated procedure was used to prepare 3D-models of all allergens where there was no experimentally determined 3D structure or high identity (95%) to another protein of known 3D structure. After a final selection by quality criteria, 433 reliable 3D models were retained and are available from our SDAP Website. The new 3D models extensively enhance our knowledge of allergen structures. As an example of their use, experimentally derived "continuous IgE epitopes" were mapped on 3 experimentally determined structures and 13 of our 3D-models of allergenic proteins. Large portions of these continuous sequences are not entirely on the surface and therefore cannot interact with IgE or other proteins. Only the surface exposed residues are constituents of "conformational IgE epitopes" which are not in all cases continuous in sequence. The surface exposed parts of the experimental determined continuous IgE epitopes showed a distinct statistical distribution as compared to their presence in typical protein-protein interfaces. The amino acids Ala, Ser, Asn, Gly and particularly Lys have a high propensity to occur in IgE binding sites. The 3D-models will facilitate further analysis of the common properties of IgE binding sites of allergenic proteins.

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Section: Resultsmentioning

confidence: 99%

Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes

Oezguen

Zhou

Negi

et al. 2008

Molecular Immunology

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“…In order to analyze the B-cell epitopes from Asp f 13, the protein was chemically and enzymatically cleaved and subsequently the N-terminal sequences were determined. At the end, 3 of 13 linear epitopes located at the C-terminus were proven to be immunodominant [95]. …”

Section: Fungal Allergensmentioning

confidence: 99%

The Spectrum of Fungal Allergy

Simon-Nobbe¹,

Denk²,

Pöll³

et al. 2007

Int Arch Allergy Immunol

429

425

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Fungi can be found throughout the world. They may live as saprophytes, parasites or symbionts of animals and plants in indoor as well as outdoor environment. For decades, fungi belonging to the ascomycota as well as to the basidiomycota have been known to cause a broad panel of human disorders. In contrast to pollen, fungal spores and/or mycelial cells may not only cause type I allergy, the most prevalent disease caused by molds, but also a large number of other illnesses, including allergic bronchopulmonary mycoses, allergic sinusitis, hypersensitivity pneumonitis and atopic dermatitis; and, again in contrast to pollen-derived allergies, fungal allergies are frequently linked with allergic asthma. Sensitization to molds has been reported in up to 80% of asthmatic patients. Although research on fungal allergies dates back to the 19th century, major improvements in the diagnosis and therapy of mold allergy have been hampered by the fact that fungal extracts are highly variable in their protein composition due to strain variabilities, batch-to-batch variations, and by the fact that extracts may be prepared from spores and/or mycelial cells. Nonetheless, about 150 individual fungal allergens from approximately 80 mold genera have been identified in the last 20 years. First clinical studies with recombinant mold allergens have demonstrated their potency in clinical diagnosis. This review aims to give an overview of the biology of molds and diseases caused by molds in humans, as well as a detailed summary of the latest results on recombinant fungal allergens.

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“…The N-terminal sequence of gp56 showed homology to fungal serine proteases [17, 18]and not with the reported 55-kD antigen from A. fumigatus, which indicates that these proteins are different [10]. In addition, reported gp55 was shown not to possess any protease activity when fluorogenic peptide substrates were used.…”

Section: Discussionmentioning

confidence: 99%

“…Homology search of this protein sequence with other sequences available in the databank revealed a sequence similarity with a family of serine proteases. It exhibited 71 and 29% identities with serine proteases from Penicillium notatum (Pen n 13) and A. fumigatus (Asp f 13) [17, 18]. Trypsin digestion of gp56 produced eight peptides.…”

Section: Resultsmentioning

confidence: 99%

A New Glycoprotein Allergen/Antigen with the Protease Activity from <i>Aspergillus fumigatus</i>

Nigam¹,

Ghosh²,

Sarma³

2003

Int Arch Allergy Immunol

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Background:Aspergillus fumigatus is an opportunistic fungus causing allergic and invasive aspergillosis in humans and animals. It secretes an array of complex biologically active glycoprotein antigens and allergens. It is important to identify and characterize probable potential virulent factors playing a major role in the pathogenesis of aspergillosis. Methods: Using protein purification techniques (lectin affinity chromatography, gel filtration, electroelution and high-pressure liquid chromatography), a major antigen/allergen with a molecular weight of 56 kD (gp56) from A. fumigatus was purified to homogeneity. The protein was characterized by immunoblot, ELISA and protease assays. The N-terminal amino acid sequencing was performed. Results: The gp56 protein showed a single band on silver staining and isoelectric focussing. The protein to carbohydrate ratio was 1.5:1 and gp56 gave a protein band at a molecular weight of 34 kD on enzymatic deglycosylation. It also exhibited IgG and IgE immunobinding with antibodies present in sera of allergic bronchopulmonary aspergillosis patients. The gp56 exhibited protease activity and N-terminal seven-amino acid sequence showed homology with fungal serine proteases. Conclusions: The gp56 protein by virtue of its proteolytic activity could be one of the virulent factors of A. fumigatus involved in establishing infection in the host along with other factors.

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Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies

Cited by 18 publications

References 23 publications

Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes

Comprehensive 3D-modeling of allergenic proteins and amino acid composition of potential conformational IgE epitopes

The Spectrum of Fungal Allergy

A New Glycoprotein Allergen/Antigen with the Protease Activity from <i>Aspergillus fumigatus</i>

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