TY - JOUR
T1 - A crystallin fold in the interleukin-4-inducing principle of schistosoma mansoni eggs (IPSE/α-1) mediates IgE binding for antigen-independent basophil activation
AU - Meyer, N. Helge
AU - Mayerhofer, Hubert
AU - Tripsianes, Konstantinos
AU - Blindow, Silke
AU - Barths, Daniela
AU - Mewes, Astrid
AU - Weimar, Thomas
AU - Köhli, Thies
AU - Bade, Steffen
AU - Madl, Tobias
AU - Frey, Andreas
AU - Haas, Helmut
AU - Mueller-Dieckmann, Jochen
AU - Sattler, Michael
AU - Schramm, Gabriele
N1 - Publisher Copyright:
© 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2015/9/4
Y1 - 2015/9/4
N2 - Background: The interleukin-4-inducing principle from Schistosoma mansoni eggs (IPSE/α-1) triggers basophils to release interleukin-4 and interleukin-13 in an IgE-dependent but antigen-independent way. Results: Structural analysis identified IPSE/α-1 as a new member of the βγ-crystallin superfamily with a unique IgE-binding loop. Conclusion: IPSE/α-1 activates basophils via IgE-binding crystallin folds. Significance: Schistosomes use unique mechanisms to manipulate the host's immune response.
AB - Background: The interleukin-4-inducing principle from Schistosoma mansoni eggs (IPSE/α-1) triggers basophils to release interleukin-4 and interleukin-13 in an IgE-dependent but antigen-independent way. Results: Structural analysis identified IPSE/α-1 as a new member of the βγ-crystallin superfamily with a unique IgE-binding loop. Conclusion: IPSE/α-1 activates basophils via IgE-binding crystallin folds. Significance: Schistosomes use unique mechanisms to manipulate the host's immune response.
UR - http://www.scopus.com/inward/record.url?scp=84941353131&partnerID=8YFLogxK
U2 - 10.1074/jbc.M115.675066
DO - 10.1074/jbc.M115.675066
M3 - Journal articles
C2 - 26163514
AN - SCOPUS:84941353131
SN - 0021-9258
VL - 290
SP - 22111
EP - 22126
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 36
ER -
