Characterization of Major Allergens of Parietaria officinalis
- 1 January 1996
- journal article
- research article
- Published by S. Karger AG in International Archives of Allergy and Immunology
- Vol. 109 (2) , 141-149
- https://doi.org/10.1159/000237213
Abstract
The major allergens of Parietaria officinalis were characterized with a panel of nine monoclonal antibodies (mAbs). The binding of mAbs and patients’ IgE in Western blots revealed two proteins with similar molecular weights in the range of 8-10 kD. Analysis of the mAb-binding patterns in Western blots of P. officinalis extract under reducing and nonreducing conditions allows the mAbs to be divided into three different groups. mAbs of group I recognize the higher-molecular-weight component (9.4 kD), mAbs of group II recognize the lower component (8.8 kD) and mAbs of group III recognize both proteins. A comparable mAb-binding pattern was observed with Western blots of Parietaria judaica. The mAbs were used for affinity purification of the corresponding proteins from a P. officinalis extract. The purified proteins obtained with mAbs of group I–III inhibit the binding of patients’ IgE (serum pool) to a high degree, indicating that they possess the major IgE-reactive epitopes. The affinity-purified proteins were subjected to SDS-PAGE, blotted and immunologically stained by mAb binding. The results confirmed those obtained with the complete extracts. The N-terminal amino acid sequences of the blotted proteins were analyzed. The sequences of all the proteins contained highly conserved regions: GGVV (positions 4–7) and MPPLL (positions 11–15), alternating with highly variable regions (positions 1–3 for group II and 8–10 for group I). A specific group I sequence appears to be at position 1–3 with the amino acids APA and a specific group II sequence appears to be at position 8–10 with the amino acids GAL. It is possible that the two similar proteins are isoforms of Par·1.Keywords
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