Integrin B1 promotes the interaction of murine IgG3 with effector cells

Carolyn Saylor Hawk, Carolina Coelho, Diane Sthefany Lima de Oliveira, Verenice Paredes, Patrícia Albuquerque, Anamélia Lorenzetti Bocca, Ananésia Correa dos Santos, Victoria Rusakova, Heather Holemon, Ildinete Silva-Pereira, Maria Sueli Soares Felipe, Hideo Yagita, André Moraes Nicola, Arturo Casadevall

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


Abs exert several of their effector functions by binding to cell surface receptors. For murine IgG3 (mIgG3), the identity of its receptors (and the very existence of a receptor) is still under debate, as not all mIgG3 functions can be explained by interaction with FcgRI. This implies the existence of an alternate receptor, whose identity we sought to pinpoint. We found that blockage of integrin b1 selectively hampered binding of mIgG3 to macrophages and mIgG3-mediated phagocytosis. Manganese, an integrin activator, increased mIgG3 binding to macrophages. Blockage of FcgRI or Itgb1 inhibited binding of different mIgG3 Abs to variable extents. Our results are consistent with the notion that Itgb1 functions as part of an IgG receptor complex. Given the more ancient origin of integrins in comparison with FcgR, this observation could have far-ranging implications for our understanding of the evolution of Ab-mediated immunity as well as in immunity to microorganisms, pathogenesis of autoimmune diseases, and Ab engineering.

Original languageEnglish (US)
Pages (from-to)2782-2794
Number of pages13
JournalJournal of Immunology
Issue number9
StatePublished - May 1 2019

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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