Characterization of major allergens Parietaria officinalis

被引:20
作者
Kahlert, H [1 ]
Weber, B [1 ]
Teppke, M [1 ]
Wahl, R [1 ]
Cromwell, O [1 ]
Fiebig, H [1 ]
机构
[1] UNIV HAMBURG,DEPT BIOCHEM & MOLEC BIOL,HAMBURG,GERMANY
关键词
Parietaria; Parietaria officinalis; major allergen; monoclonal antibodies; allergen characterization;
D O I
10.1159/000237213
中图分类号
R392 [医学免疫学];
学科分类号
100102 ;
摘要
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 o 1.
引用
收藏
页码:141 / 149
页数:9
相关论文
共 25 条
[1]   PURIFICATION OF PAR-J-I, THE MAJOR ALLERGEN OF PARIETARIA-JUDAICA POLLEN [J].
AYUSO, R ;
POLO, F ;
CARREIRA, J .
MOLECULAR IMMUNOLOGY, 1988, 25 (01) :49-56
[2]   ISOLATION BY MAB BASED AFFINITY-CHROMATOGRAPHY OF 2 PAR J I ISOALLERGENS - COMPARISON OF THEIR PHYSICOCHEMICAL, IMMUNOCHEMICAL AND ALLERGENIC PROPERTIES [J].
AYUSO, R ;
CARREIRA, J ;
LOMBARDERO, M ;
DUFFORT, O ;
PERIS, A ;
BASOMBA, A ;
POLO, F .
MOLECULAR IMMUNOLOGY, 1993, 30 (15) :1347-1354
[3]  
AYUSO R, 1993, ALLERGY S16, V48, P129
[4]  
CHAPMAN MD, 1988, ALLERGY S5, V42, P7
[5]   PURIFICATION OF PAR-J-I, A MAJOR ALLERGEN FROM PARIETARIA-JUDAICA POLLEN [J].
COCCHIARA, R ;
LOCOROTONDO, G ;
PARLATO, A ;
GUARNOTTA, G ;
RONCHI, S ;
ALBEGGIANI, G ;
AMOROSO, S ;
FALAGIANI, P ;
GERACI, D .
INTERNATIONAL ARCHIVES OF ALLERGY AND APPLIED IMMUNOLOGY, 1989, 90 (01) :84-90
[6]   ISOLATION OF THE MAJOR IGE-BINDING PROTEIN FROM PARIETARIA-JUDAICA POLLEN USING MONOCLONAL-ANTIBODIES [J].
CORBI, AL ;
LEY, V ;
SANCHEZMADRID, F ;
CARREIRA, J .
MOLECULAR IMMUNOLOGY, 1985, 22 (09) :1081-1089
[7]  
CORBI AL, 1985, ANN ALLERGY, V54, P142
[8]  
COSTA MA, 1994, FEBS LETT, V341, P2
[9]   PARIETARIA POLLINOSIS - A REVIEW [J].
DAMATO, G ;
RUFFILLI, A ;
SACERDOTI, G ;
BONINI, S .
ALLERGY, 1992, 47 (05) :443-449
[10]   POLLEN-RELATED ALLERGY IN THE EUROPEAN MEDITERRANEAN AREA [J].
DAMATO, G ;
LICCARDI, G .
CLINICAL AND EXPERIMENTAL ALLERGY, 1994, 24 (03) :210-219