نتایج جستجو برای: fcγriiia
تعداد نتایج: 216 فیلتر نتایج به سال:
Removal of the fucose residue from the N-glycans of the Fc portion of immunoglobulin G (IgG) results in a dramatic enhancement of antibody-dependent cellular cytotoxicity (ADCC) through improved affinity for Fcγ receptor IIIa (FcγRIIIa). Here, we present the 2.2-Å structure of the complex formed between nonfucosylated IgG1-Fc and a soluble form of FcγRIIIa (sFcγRIIIa) with two N-glycosylation s...
IgG1 Fc is a remarkable molecule, capable of initiating pro-inflammatory or antiinflammatory responses by binding to Fc receptors. IgG1 Fc has a conserved glycosylation site at N297. The presence of the carbohydrate at N297 is vital for proper Fc function. Intramolecular glycan-polypeptide interactions are thought to impose conformational restrictions on Fc that maintain binding-favorable inter...
Neutralizing (nAbs) and high affinity binding antibodies may be critical for an efficacious HIV-1 vaccine. We characterized virus-specific nAbs and binding antibody responses over 21 months in eight HIV-1 subtype C chronically infected individuals with heterogeneous rates of disease progression. Autologous nAb titers of study exit plasma against study entry viruses were significantly higher tha...
Background: Multiple Sclerosis (MS), the most common demyelinating disease of the CNS, is immunologically mediated in genetically susceptible individuals. Receptors for the Fc fragment of IgG (FcγR) might induce inflammatory responses through linking the humoral and cellular immune responses by targeting immune complexes to effector cells. Polymorphisms in some FcγR genes are associated with va...
Purpose: This study was undertaken to evaluate the effects of MDX-1401, a nonfucosylated fully human monoclonal antibody that binds to human CD30, and to determine whether it exhibits greater in vitro and in vivo activity than its parental antibody. Experimental Design: Assaysmeasuring antibody binding to CD30-expressing cells and FcγRIIIa (CD16) transfectants as well as antibody-dependent cell...
Kenkre and colleagues report the absence of correlation between FcγRIIIa-V158F polymorphism and rituximab response in follicular lymphoma patients, a result which is in contrast with prior studies. This discrepancy recalls that many other factors (from the host and from the tumor) may influence the efficacy of rituximab in vivo.
Fcγ receptors (FcγRs) on effector cells are of importance for mediating antibody-dependent cellular cytotoxicity (ADCC). FcγRIIIa158valine (V)/phenylalanine (F) and FcγRIIa131histidine (H)/arginine(R) polymorphisms have been shown to relate to prognosis in antibody-treated patients. The aim of the present study was to analyze the polymorphisms of both FcγRIIIa and FcγRIIa in colorectal carcinom...
PURPOSE FcγR polymorphisms have been reported to enhance the immune-mediated effects of cetuximab in metastatic colorectal cancer. There are no data on the relationship between these polymorphisms and cetuximab in the early-stage setting. We performed a pharmacogenomic analysis of EXPERT-C, a randomized phase II trial of neoadjuvant CAPOX followed by chemoradiotherapy, surgery, and adjuvant CAP...
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