IgG Immune Complexes Inhibit Naïve T Cell Proliferation and Suppress Effector Function in Cytotoxic T Cells

Autor: Wissam Charab, Matthew G. Rosenberger, Haridha Shivram, Justin M. Mirazee, Moses Donkor, Soumya R. Shekhar, Donjeta Gjuka, Kimberly H. Khoo, Jin Eyun Kim, Vishwanath R. Iyer, George Georgiou

Publikováno v: Frontiers in Immunology, Vol 12 (2021)

Elevated levels of circulating immune complexes are associated with autoimmunity and with worse prognoses in cancer. Here, we examined the effects of well-defined, soluble immune complexes (ICs) on human peripheral T cells. We demonstrate that IgG-IC

Externí odkaz: https://doaj.org/article/c049867e177140afbbee7adb7f333a2e

IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions

Autor: Bianca Balbino, George Delidakis, Tae Hyun Kang, Makiko Watanabe, Kendra Triplett, Anja Lux, Navin Varadarajan, Odile Richard-Le Goff, Oana I. Lungu, Pierre Bruhns, George Georgiou, Corrine Alford, Gabrielle Romain, Margaret A. Lindorfer, Wissam Charab, Falk Nimmerjahn, Yan Jessie Zhang, Hidetaka Tanno, Wupeng Yan, Nicholas M. Marshall, Moses Donkor, Chang-Han Lee, Jiwon Lee, Ronald P. Taylor, Biliana Todorova

Publikováno v: Nature Immunology
Nature Immunology, Nature Publishing Group, 2017, 18 (8), pp.889-898. ⟨10.1038/ni.3770⟩
Nature Immunology, 2017, 18 (8), pp.889-898. ⟨10.1038/ni.3770⟩

International audience; Engineered crystallizable fragment (Fc) regions of antibody domains, which assume a unique and unprecedented asymmetric structure within the homodimeric Fc polypeptide, enable completely selective binding to the complement com

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3d0740466da17325dc05af13c9b0b13
https://hal-pasteur.archives-ouvertes.fr/pasteur-02510289

Erratum: Corrigendum: IgG Fc domains that bind C1q but not effector Fcγ receptors delineate the importance of complement-mediated effector functions

Autor: Corrine Alford, Gabrielle Romain, Margaret A. Lindorfer, Falk Nimmerjahn, Wissam Charab, Moses Donkor, Navin Varadarajan, George Delidakis, Bianca Balbino, Anja Lux, Hidetaka Tanno, Wupeng Yan, Ronald P. Taylor, Kendra Triplett, Pierre Bruhns, Odile Richard-Le Goff, Chang-Han Lee, Tae Hyun Kang, George Georgiou, Oana I. Lungu, Biliana Todorova, Jiwon Lee, Nicholas M. Marshall, Makiko Watanabe, Yan Jessie Zhang

Publikováno v: Nature Immunology. 18:1173-1173

Nat. Immunol.; doi:10.1038/ni.3770; corrected online 27 June 2017 In the version of this article initially published online, the labels identifying each plot in Figure 1b were missing. The labels are as follows (left to right): CHO, FcγRI, FcγRIIaR

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f5f79ee572f1bfaadfc4cf5f530fe426
https://doi.org/10.1038/ni1017-1173c

IgGA: a 'cross-isotype' engineered human Fc antibody domain that displays both IgG-like and IgA-like effector functions

Autor: Wissam Charab, Nishant Mehta, Takaaki Kojima, Tae Hyun Kang, William Kelton, Chang-Han Lee, George Georgiou, Jiwon Lee

Publikováno v: Chemistrybiology. 21(12)

SummaryAll clinically approved antibodies are of the IgG isotype and mediate the clearance of target cells via binding to Fcγ receptors and complement (C1q). Even though IgA can elicit powerful cytotoxic action via FcαRI receptor binding, IgA antib

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::568a82626163487ff1f426a5db45323b
https://pubmed.ncbi.nlm.nih.gov/25500223