A crystallin fold in the interleukin-4-inducing principle of schistosoma mansoni eggs (IPSE/α-1) mediates IgE binding for antigen-independent basophil activation

  • N. Helge Meyer
  • , Hubert Mayerhofer
  • , Konstantinos Tripsianes
  • , Silke Blindow
  • , Daniela Barths
  • , Astrid Mewes
  • , Thomas Weimar
  • , Thies Köhli
  • , Steffen Bade
  • , Tobias Madl
  • , Andreas Frey
  • , Helmut Haas
  • , Jochen Mueller-Dieckmann
  • , Michael Sattler
  • , Gabriele Schramm

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)22111-22126
Number of pages16
JournalJournal of Biological Chemistry
Volume290
Issue number36
DOIs
StatePublished - 4 Sep 2015

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