Lys89, Lys90, and Phe91 are critical core amino acid residues of the Pen ch 18 major fungal allergen recognized by human IgE antibodies
| Autor: | Hong Chou, Ming F. Tam, Horng-Der Shen, Hsiao-Yun Tai, Tien-Tien Cheng |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
Protein Conformation
Phenylalanine Biophysics Penicillium chrysogenum Immunoglobulin E medicine.disease_cause Biochemistry Epitope Fungal Proteins Allergen medicine Humans Molecular Biology Antibodies Fungal Alanine Serine protease Fungal protein biology Immunodominant Epitopes Chemistry Lysine Cell Biology Allergens biology.organism_classification Recombinant Proteins Epitope mapping Mutation biology.protein Epitope Mapping |
| Zdroj: | Biochemical and Biophysical Research Communications. 375:671-674 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2008.08.097 |
| Popis: | A vacuolar serine protease (Pen ch 18) has been identified as a major allergen of Penicillium chrysogenum. The molecular features of antigenic determinant(s) on Pen ch 18 recognized by human IgE antibodies, however, have remained unclear. Here, we show that a dominant IgE epitope on the N-terminally processed Pen ch 18 allergen was narrowed down to residues 83-91. In addition, Lys89, Lys90, and possibly Phe91 were identified as the core residues. Substitution of Lys89, Lys90, or Phe91 with alanine can significantly reduce IgE-binding to Pen ch 18. Immunoblot inhibition confirmed that Lys89 and Phe91 played a significant role in IgE-binding against Pen ch 18. Molecular modeling suggests they are located on a loop-like structure at or near the surface of the major fungal allergen. |
| Databáze: | OpenAIRE |
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