Abstract
We report the characterization of a domain of the major timothy grass pollen allergen, Phl p 5A, which contains the binding site for a human monoclonal IgE antibody. The human monoclonal IgE antibody fragment (Fab) was obtained from an IgE combinatorial library constructed from lymphocytes of a grass pollen-allergic patient. An 11.2-kD N-terminal fragment representing approximately one third of the complete Phl p 5A allergen could be identified to contain the binding site for the IgE Fab. The rPhl p 5A fragment revealed an extremely high allergenic activity in skin test experiments which in some cases equaled that of the complete Phl p 5A allergen. The rPhl p 5A domain thus represents an allergen fragment containing several IgE epitopes in a configuration optimal for efficient effector cell activation. We suggest the rPhl p 5A fragment and the corresponding IgE Fab as paradigmatic tools to explore the structural requirements for highly efficient effector cell activation.
| Original language | English |
|---|---|
| Pages (from-to) | 80-84 |
| Number of pages | 5 |
| Journal | International Archives of Allergy and Immunology |
| Volume | 124 |
| Issue number | 1-3 |
| DOIs | |
| Publication status | Published - 2001 |
| Externally published | Yes |
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Keywords
- Allergen
- Epitope
- Monoclonal human IgE
ASJC Scopus subject areas
- Immunology and Allergy
- Immunology
Cite this
A highly allergenic fragment of the major timothy grass pollen allergen, Phl p 5, defined by a human monoclonal IgE antibody. / Flicker, S.; Vrtala, S.; Steinberger, P.; Vangelista, L.; Kraft, D.; Valenta, Rudolf.
In: International Archives of Allergy and Immunology, Vol. 124, No. 1-3, 2001, p. 80-84.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A highly allergenic fragment of the major timothy grass pollen allergen, Phl p 5, defined by a human monoclonal IgE antibody
AU - Flicker, S.
AU - Vrtala, S.
AU - Steinberger, P.
AU - Vangelista, L.
AU - Kraft, D.
AU - Valenta, Rudolf
PY - 2001
Y1 - 2001
N2 - We report the characterization of a domain of the major timothy grass pollen allergen, Phl p 5A, which contains the binding site for a human monoclonal IgE antibody. The human monoclonal IgE antibody fragment (Fab) was obtained from an IgE combinatorial library constructed from lymphocytes of a grass pollen-allergic patient. An 11.2-kD N-terminal fragment representing approximately one third of the complete Phl p 5A allergen could be identified to contain the binding site for the IgE Fab. The rPhl p 5A fragment revealed an extremely high allergenic activity in skin test experiments which in some cases equaled that of the complete Phl p 5A allergen. The rPhl p 5A domain thus represents an allergen fragment containing several IgE epitopes in a configuration optimal for efficient effector cell activation. We suggest the rPhl p 5A fragment and the corresponding IgE Fab as paradigmatic tools to explore the structural requirements for highly efficient effector cell activation.
AB - We report the characterization of a domain of the major timothy grass pollen allergen, Phl p 5A, which contains the binding site for a human monoclonal IgE antibody. The human monoclonal IgE antibody fragment (Fab) was obtained from an IgE combinatorial library constructed from lymphocytes of a grass pollen-allergic patient. An 11.2-kD N-terminal fragment representing approximately one third of the complete Phl p 5A allergen could be identified to contain the binding site for the IgE Fab. The rPhl p 5A fragment revealed an extremely high allergenic activity in skin test experiments which in some cases equaled that of the complete Phl p 5A allergen. The rPhl p 5A domain thus represents an allergen fragment containing several IgE epitopes in a configuration optimal for efficient effector cell activation. We suggest the rPhl p 5A fragment and the corresponding IgE Fab as paradigmatic tools to explore the structural requirements for highly efficient effector cell activation.
KW - Allergen
KW - Epitope
KW - Monoclonal human IgE
UR - http://www.scopus.com/inward/record.url?scp=0035053093&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035053093&partnerID=8YFLogxK
U2 - 10.1159/000053675
DO - 10.1159/000053675
M3 - Article
VL - 124
SP - 80
EP - 84
JO - International Archives of Allergy and Immunology
JF - International Archives of Allergy and Immunology
SN - 1018-2438
IS - 1-3
ER -