The cell surface protein CD83 belongs to the immunoglobulin superfamily and is highly expressed on mature dendritic cells. The soluble form of CD83, sCD83, is a potential immune suppressor. In a previous study, recombinant soluble CD83 was expressed in Escherichia coli, resulting in a lack of functional glycosylation.
Lin Wan, Wan Lin
exaly +6 more sources
Engineering the fragment crystallizable (Fc) region of human IgG1 multimers and monomers to fine-tune interactions with sialic acid-dependent receptors [PDF]
Multimeric fragment crystallizable (Fc) regions and Fc-fusion proteins are actively being explored as biomimetic replacements for IVIG therapy, which is deployed to manage many diseases and conditions but is expensive and not always efficient. The Fc region of human IgG1 (IgG1-Fc) can be engineered into multimeric structures (hexa-Fcs) that bind their ...
Richard Pleass +2 more
exaly +5 more sources
The therapeutic potential of sialylated fragment crystallizable (Fc) domains of human IgG [PDF]
Pathogens frequently use multivalent binding to sialic acid to infect cells or to modulate immunity through interactions with human sialic acid-binding immunoglobulin-type lectins (Siglecs).
Pleass, Richard
core +3 more sources
A Method to Detect the Binding of Hyper-Glycosylated Fragment Crystallizable (Fc) Region of Human IgG1 to Glycan Receptors [PDF]
Engineering the fragment crystallizable (Fc) of human IgG can bring improved effector functions to monoclonal antibodies and Fc-fusion-based medicines and vaccines. Such Fc-effector functions are largely controlled by posttranslational modifications (PTMs) within the Fc, including the addition of glycans that introduce structural and functional ...
Patricia, Blundell, Richard, Pleass
openaire +4 more sources
AbstractShort half-lives in circulation and poor transport across the blood–brain barrier limit the utility of cytokines and growth factors acting as receptor agonists. Here we show that surrogate receptor agonists with longer half-lives in circulation and enhanced transport rates across the blood–brain barrier can be generated by genetically inserting
Katsuya Sakai +2 more
exaly +3 more sources
Chimeric single-chain variable fragment-human immunoglobulin G crystallizable fragment antibody against GD2 for neuroblastoma targeted immunotherapy [PDF]
Aim: The present study aims to generate chimeric mouse single-chain variable fragment (scFv) and immunoglobulin G1 (IgG1) crystallizable fragment (Fc) antibody against disialoganglioside (GD2) for the treatment of neuroblastoma (NB).
Supansa Pata +2 more
exaly +2 more sources
An interesting format in the development of therapeutic monoclonal antibodies uses the crystallizable fragment of IgG1 as starting scaffold. Engineering of its structural loops allows generation of an antigen binding site.
Balder Lai +2 more
exaly +2 more sources
The N-Glycosylation of Mouse Immunoglobulin G (IgG)-Fragment Crystallizable Differs Between IgG Subclasses and Strains [PDF]
N-linked glycosylation of the fragment crystallizable (Fc)-region of immunoglobulin G (IgG) is known to have a large influence on the activity of the antibody, an effect reported to be IgG subclass specific. This situation applies both to humans and mice.
Noortje de Haan +2 more
exaly +2 more sources
The Development of Launch Methods for High Velocity Fragment Simulating Projectiles [PDF]
This paper describes the development of small-scale high velocity fragment launch methods which might be used to reproduce the effect of EFP-IED warheads.
Horsfall, Ian, McCamphill-Rose, P. J.
core +7 more sources
Choice of host cell line is essential for the functional glycosylation of the fragment crystallizable (Fc) region of human IgG1 inhibitors of influenza B viruses [PDF]
Abstract Antibodies are glycoproteins that carry a conserved N-linked carbohydrate attached to the Fc, whose presence and fine structure profoundly impacts on their in vivo immunogenicity, pharmacokinetics and functional attributes. The host cell line used to produce IgG has a major
Blundell, Patricia A. +4 more
openaire +1 more source

