Sentence examples for binding to human FcRn from inspiring English sources

Screening of a phage display Fc variant library identified mutations (e.g., M252Y/S254T/T256E termed YTE) with enhanced binding to human FcRn at pH 6.0 (Dall'Acqua et al., 2002).

Here, we show that G1Δnab mutants retain pH-dependent binding to human FcRn but that the amino acid alterations reduce the affinity of the IgG1 FcRn interaction by 2.0-fold and 1.6-fold for the two antibodies investigated.

A later study demonstrated that the YTE variant had 10-fold increased binding to human and cynomolgus FcRn at pH 6.0, which translated into a 4-fold increase in half-life in a cynomolgus PK study (Dall'Acqua et al., 2006).

Binding to human CD64 (the high-affinity activating FcγR) and FcRn (the neonatal FcγR) is not substantially modified.

However, significantly different clearance values are expected in human patients, since human FcRn binds to human but not to mouse IgG, resulting in longer retention of the chAb in the blood [37].

For FcRn binding, recombinant human FcRn was biotinylated enzymatically using a C-terminal Avi-tag sequence.

In this study, five Fc variants known to enhance human FcRn (hFcRn) binding with mutations in the CH2 and/or CH3 domains were constructed on a humanized version of E6F6 (huE6F6), a novel therapeutic mAb against HBV.

When introduced into the CH2 domain of human immunoglobulin G (IgG) molecules, the triple mutation M252Y/S254T/T256E ('YTE') causes an about 10-fold increase in their binding to the human neonatal Fc receptor (FcRn).

The circulating half-life of IgG2σ in monkeys is extended relative to IgG1 and IgG2, in spite of similar in vitro binding to recombinant FcRn.

For example, design monomeric or polymeric Fc-fusions with selective binding to FcRs, FcRn or FcRLs.

Albumin also maintains long circulating half-life by a similar binding to the FcRn.