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

Abstract：

: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 component C1q and activation of complement via the classical pathway without any concomitant engagement of the Fcγ receptor (FcγR). We used the engineered Fc domains to demonstrate in vitro and in mouse models that for therapeutic antibodies, complement-dependent cell-mediated cytotoxicity (CDCC) and complement-dependent cell-mediated phagocytosis (CDCP) by immunological effector molecules mediated the clearance of target cells with kinetics and efficacy comparable to those of the FcγR-dependent effector functions that are much better studied, while they circumvented certain adverse reactions associated with FcγR engagement. Collectively, our data highlight the importance of CDCC and CDCP in monoclonal-antibody function and provide an experimental approach for delineating the effect of complement-dependent effector-cell engagement in various therapeutic settings.

journal_name

Nat Immunol

journal_title

Nature immunology

authors

Lee CH,Romain G,Yan W,Watanabe M,Charab W,Todorova B,Lee J,Triplett K,Donkor M,Lungu OI,Lux A,Marshall N,Lindorfer MA,Goff OR,Balbino B,Kang TH,Tanno H,Delidakis G,Alford C,Taylor RP,Nimmerjahn F,Varadarajan N,

doi

10.1038/ni.3770

subject

Has Abstract

pub_date

2017-08-01 00:00:00

pages

889-898

issue

8

eissn

1529-2908

issn

1529-2916

pii

ni.3770

journal_volume

18

pub_type

杂志文章

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