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Characterization of major allergens of Parietaria officinalis.

Authors
  • Kahlert, H
  • Weber, B
  • Teppke, M
  • Wahl, R
  • Cromwell, O
  • Fiebig, H
Type
Published Article
Journal
International archives of allergy and immunology
Publication Date
Feb 01, 1996
Volume
109
Issue
2
Pages
141–149
Identifiers
PMID: 8563489
Source
Medline
License
Unknown

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 posses 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 o 1.

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