| First Author | Hawk CS | Year | 2019 |
| Journal | J Immunol | Volume | 202 |
| Issue | 9 | Pages | 2782-2794 |
| PubMed ID | 30894426 | Mgi Jnum | J:274902 |
| Mgi Id | MGI:6296873 | Doi | 10.4049/jimmunol.1701795 |
| Citation | Hawk CS, et al. (2019) Integrin beta1 Promotes the Interaction of Murine IgG3 with Effector Cells. J Immunol 202(9):2782-2794 |
| abstractText | 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 FcgammaRI. This implies the existence of an alternate receptor, whose identity we sought to pinpoint. We found that blockage of integrin beta1 selectively hampered binding of mIgG3 to macrophages and mIgG3-mediated phagocytosis. Manganese, an integrin activator, increased mIgG3 binding to macrophages. Blockage of FcgammaRI 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 FcgammaR, 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. |
