2000
DOI: 10.1016/s0165-2478(99)00140-6
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Expression of an epitopic region of AspfI, an allergen/antigen/cytotoxin of Aspergillus fumigatus

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Cited by 9 publications
(8 citation statements)
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“…However, Kurup et al showed that three peptides from the C terminus of Asp f 1 significantly inhibited IgE binding of Asp f 1 (inhibition ranged from 80 to 100%) (18). In an earlier study, a recombinant N-terminal fragment of Asp f 1 (8 to 45 amino acid residues), which comprised the immunodominant region of the present study, showed binding to specific IgG and IgE antibodies in ABPA patients by immunoblotting and ELISA (29).…”
Section: Discussionsupporting
confidence: 45%
See 1 more Smart Citation
“…However, Kurup et al showed that three peptides from the C terminus of Asp f 1 significantly inhibited IgE binding of Asp f 1 (inhibition ranged from 80 to 100%) (18). In an earlier study, a recombinant N-terminal fragment of Asp f 1 (8 to 45 amino acid residues), which comprised the immunodominant region of the present study, showed binding to specific IgG and IgE antibodies in ABPA patients by immunoblotting and ELISA (29).…”
Section: Discussionsupporting
confidence: 45%
“…The National Center for Biotechnology Information protein BLAST tool for short sequences in fungi showed that P1 has complete sequence similarity only to Asp f 1 and related ribotoxins of other Aspergillus species (E value, 1e-04) and partial similarity to elongation factor 2 of various species of Saccharomyces and Candida (only 7 out of 11 amino acid residues were identical, with an E value of 4.3). The comparable sensitivity of P1 to that of SDA may be due to the presence of homologous IgG binding epitopes in six immunodominant allergens and antigens (24,29,55,66,77, and 88 kDa) and homologous IgE binding epitopes in three immunodominant allergens and antigens (27,34, and 43 kDa) besides Asp f 1 (28).…”
Section: Discussionmentioning
confidence: 94%
“…We note the presence of a low homology orthologues of Asp f 1 in the A. terreus genome – an organism previously reported to have no cross reactivity to Asp f 1 [ 29 ]. Hence we examined the predicted structure and epitopes of Asp f 1 and its orthologues to determine whether Asp f 1 epitope orthologues were conserved and whether the orthologues from A. terreus would be predicted to contain credible epitope orthologues using our approach [ 44 , 45 ].…”
Section: Resultsmentioning
confidence: 99%
“…A. fumigatus produces a protein toxin Asp f1 with multiple functions. It is an important allergen, antigen, has ribonuclease activity and is highly cytotoxic [31,32]. A. fumigatus also produces Asp-hemolysin which induces hemolysis of erythrocytes [33].…”
Section: Bioactive Molecules Of Aspergillus Speciesmentioning
confidence: 99%