Tryptophan residue is essential for immunoreactivity of a diagnostically relevant peptide epitope of A. fumigatus |
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| Authors: | Neel Kamal Shantanu Chowdhury Taruna Madan Deepak Sharma M Attreyi Wahajul Haq Seturam Bandacharya Katti Anil Kumar P Usha Sarma |
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| Institution: | (1) Institute of Genomics and Integrative Biology, Mall Road, Delhi, India;(2) Department of Chemistry, University of Delhi, Delhi, India;(3) Biopolymers Division, Central Drug Research Institute, Lucknow, India;(4) School of Biotechnology, Devi Ahilya Vishwavidyalaya, Khandwa Road, Indore, India;(5) Present address: Biology Department, Boston College, Chestnut Hill, Massachusetts, U.S.A.;(6) Present address: Department of Plant Pathology, Indian Agricultural Research Institute, Delhi, India;(7) Molecular Biochemistry and Diagnostics Division, Institute of Genomics and Integrative Biology, Mall Road, Delhi-7, India |
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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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| Keywords: | allergic bronchopulmonary aspergillosis Aspergillus fumigatus BIAcore immunoreactivity peptide tryptophan |
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