ArticleMolecular and cellular biochemistry2005
Tryptophan residue is essential for immunoreactivity of a diagnostically relevant peptide epitope of A. fumigatus.
Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 6 citations in OpenAlex.
- Prophylactic and Therapeutic Potential of Asp f1 Epitopes in Naïve and Sensitized BALB/c Mice.Immune network · 2009Article
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9 authors at 4 institutions in 1 country.
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Abstract
The role of tryptophan (Trp17) in immunoreactivity of P1, the diagnostically relevant peptide from a major allergen/antigen of Aspergillus fumigatus, was evaluated by chemically modifying tryptophanyl residue of P1. In BIAcore kinetic studies, unmodified P1 showed a 100-fold higher binding with ABPA (Allergic Bronchopulmonary Aspergillosis) patients' IgG [KD (equilibrium dissociation constant) = 2.74 e(-8) +/- 0.13 M] than the controls' IgG (KD = 2.97 e(-6) +/- 0.14 M), whereas chemically-modified P1 showed similar binding [KD patients' IgG = 3.25 e(-7) +/- 0.16 M, KD controls' IgG = 3.86 e(-7) +/- 0.19 M] indicating loss of specific immunoreactivity of P1 on tryptophan modification. Modified P1 showed loss of specific binding to IgE and IgG antibodies of ABPA patients in ELISA (Enzyme-Linked Immunosorbent Assay). The study infers that tryptophan residue (Trp17) is essential for immunoreactivity of P1.
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