Immunoglobulin G1 Fc Domain Motions: Implications for Fc Engineering
نویسندگان
چکیده
منابع مشابه
Aglycosylated immunoglobulin G1 variants productively engage activating Fc receptors.
Immunoglobulin G plays a vital role in adaptive immunity and antibody-based therapy through engagement of its Fc region by the Fc gamma receptors (Fc gammaRs) on immune cells. In addition to specific protein-protein contacts, N-linked glycosylation of the IgG Fc has been thought to be essential for the recognition of Fc by Fc gammaR. This requirement for the N-linked glycan has limited biomanuf...
متن کاملEngineering of Immunoglobulin Fc Heterodimers Using Yeast Surface-Displayed Combinatorial Fc Library Screening
Immunoglobulin Fc heterodimers, which are useful scaffolds for the generation of bispecific antibodies, have been mostly generated through structure-based rational design methods that introduce asymmetric mutations into the CH3 homodimeric interface to favor heterodimeric Fc formation. Here, we report an approach to generate heterodimeric Fc variants through directed evolution combined with yea...
متن کاملRECEPTOR FOR IMMUNOGLOBULIN Fc ON PROTOZOA
The mechanisms parasites have developed to escape immune surveillance are currently under investigation in many laboratories, because their elucidation may provide new approaches to the prevention of the diseases the parasites cause. For a detailed description and experimental evidence of these various mechanisms, see the recent review by Bloom (1). One possible means of evasion is the uptake o...
متن کاملHuman IgG Fc domain engineering enhances antitoxin neutralizing antibody activity.
The effector activity of antibodies is dependent on engagement with Fcγ receptors (FcγRs) and activation of the associated intracellular signaling pathways. Preclinical evaluation of therapeutic humanized or chimeric mAbs to study the interactions of their Fc regions with FcγRs is hampered by substantial structural and functional FcγR diversity among species. In this report, we used mice expres...
متن کاملStructural comparison of fucosylated and nonfucosylated Fc fragments of human immunoglobulin G1.
Removal of the fucose residue from the oligosaccharides attached to Asn297 of human immunoglobulin G1 (IgG1) results in a significant enhancement of antibody-dependent cellular cytotoxicity (ADCC) via improved IgG1 binding to Fcgamma receptor IIIa. To provide structural insight into the mechanisms of affinity enhancement, we determined the crystal structure of the nonfucosylated Fc fragment and...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2014
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2014.01.011