Abstract
We constructed a soluble minimal receptor-Ig chimera in which the two extracellular domains of human FcεRI α-chain (D1 and D2) were fused to the dimerizing C-terminal domain of human IgG1 heavy chain (γ1-CH3). The protein was expressed and actively secreted by Chinese hamster ovary (CHO) cells as a fully glycosylated soluble dimeric protein. It showed efficient binding both to human membrane-bound IgE isoforms and to the two secretory IgE isoforms. Moreover, the dimeric receptor binds IgE with the expected 1:2 stoichiometry. The receptor-Ig chimera, in 2-fold molar excess, inhibited engagement of secretory IgE to rat basophilic leukemia cells expressing the human αβγ receptor. Full self-nature and inability to bind Fcγ receptors make this protein an attractive candidate for clinical applications and a novel biotechnological tool for atopic allergy research.
| Original language | English |
|---|---|
| Pages (from-to) | 51-57 |
| Number of pages | 7 |
| Journal | Protein Engineering |
| Volume | 15 |
| Issue number | 1 |
| Publication status | Published - 2002 |
| Externally published | Yes |
Fingerprint
Keywords
- Binding
- Chimera
- Dimerization
- FcεRI
- IgE
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
Cite this
A minimal receptor-Ig chimera of human FcεRI α-chain efficiently binds secretory and membrane IgE. / Vangelista, Luca; Cesco-Gaspere, Michela; Lorenzi, Roberto; Burrone, Oscar.
In: Protein Engineering, Vol. 15, No. 1, 2002, p. 51-57.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A minimal receptor-Ig chimera of human FcεRI α-chain efficiently binds secretory and membrane IgE
AU - Vangelista, Luca
AU - Cesco-Gaspere, Michela
AU - Lorenzi, Roberto
AU - Burrone, Oscar
PY - 2002
Y1 - 2002
N2 - We constructed a soluble minimal receptor-Ig chimera in which the two extracellular domains of human FcεRI α-chain (D1 and D2) were fused to the dimerizing C-terminal domain of human IgG1 heavy chain (γ1-CH3). The protein was expressed and actively secreted by Chinese hamster ovary (CHO) cells as a fully glycosylated soluble dimeric protein. It showed efficient binding both to human membrane-bound IgE isoforms and to the two secretory IgE isoforms. Moreover, the dimeric receptor binds IgE with the expected 1:2 stoichiometry. The receptor-Ig chimera, in 2-fold molar excess, inhibited engagement of secretory IgE to rat basophilic leukemia cells expressing the human αβγ receptor. Full self-nature and inability to bind Fcγ receptors make this protein an attractive candidate for clinical applications and a novel biotechnological tool for atopic allergy research.
AB - We constructed a soluble minimal receptor-Ig chimera in which the two extracellular domains of human FcεRI α-chain (D1 and D2) were fused to the dimerizing C-terminal domain of human IgG1 heavy chain (γ1-CH3). The protein was expressed and actively secreted by Chinese hamster ovary (CHO) cells as a fully glycosylated soluble dimeric protein. It showed efficient binding both to human membrane-bound IgE isoforms and to the two secretory IgE isoforms. Moreover, the dimeric receptor binds IgE with the expected 1:2 stoichiometry. The receptor-Ig chimera, in 2-fold molar excess, inhibited engagement of secretory IgE to rat basophilic leukemia cells expressing the human αβγ receptor. Full self-nature and inability to bind Fcγ receptors make this protein an attractive candidate for clinical applications and a novel biotechnological tool for atopic allergy research.
KW - Binding
KW - Chimera
KW - Dimerization
KW - FcεRI
KW - IgE
UR - http://www.scopus.com/inward/record.url?scp=0036190410&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036190410&partnerID=8YFLogxK
M3 - Article
VL - 15
SP - 51
EP - 57
JO - Protein Engineering, Design and Selection
JF - Protein Engineering, Design and Selection
SN - 1741-0126
IS - 1
ER -