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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