Cross-reactivity of IgE antibodies to allergens

Allergy ◽  
2001 ◽  
Vol 56 (6) ◽  
pp. 478-490 ◽  
Author(s):  
R. C. Aalberse ◽  
J. Akkerdaas ◽  
R. van Ree
2013 ◽  
Vol 132 (3) ◽  
pp. 639-647 ◽  
Author(s):  
Abena S. Amoah ◽  
Benedicta B. Obeng ◽  
Irene A. Larbi ◽  
Serge A. Versteeg ◽  
Yvonne Aryeetey ◽  
...  

1976 ◽  
Vol 58 (1) ◽  
pp. 129-139 ◽  
Author(s):  
Kristin M. Leiferman ◽  
Gerald J. Gleich

1976 ◽  
Vol 58 (1) ◽  
pp. 140-148 ◽  
Author(s):  
Kristin M. Leiferman ◽  
Gerald J. Gleich ◽  
Richard T. Jones

Science ◽  
2018 ◽  
Vol 362 (6420) ◽  
pp. 1306-1309 ◽  
Author(s):  
Derek Croote ◽  
Spyros Darmanis ◽  
Kari C. Nadeau ◽  
Stephen R. Quake

Immunoglobulin E (IgE) antibodies protect against helminth infections but can also cause life-threatening allergic reactions. Despite their role in human health, the cells that produce these antibodies are rarely observed and remain enigmatic. We isolated single IgE B cells from individuals with food allergies and used single-cell RNA sequencing to elucidate the gene expression and splicing patterns unique to these cells. We identified a surprising example of convergent evolution in which IgE antibodies underwent identical gene rearrangements in unrelated individuals. Through the acquisition of variable region mutations, these IgE antibodies gained high affinity and unexpected cross-reactivity to the clinically important peanut allergens Ara h 2 and Ara h 3. These findings provide insight into IgE B cell transcriptomics and enable biochemical dissection of this antibody class.


1989 ◽  
Vol 84 (2) ◽  
pp. 174-183 ◽  
Author(s):  
V.L. Koshte ◽  
S.L. Kagen ◽  
R.C. Aalberse

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