Jul 1, 2022 · We find that a CD22-targeting CAR harboring a CD8α hinge (H) exhibits greater cytotoxicity against a low antigen density CD22 + leukemia as compared to an equivalent CAR with a CD28 H. We therefore studied the biophysical and dynamic properties of the CD8α H by nuclear magnetic resonance (NMR) spectroscopy.

May 9, 2020 · However, CARs with a CD8α- or CD28-derived hinge domain showed significant differences in CAR-T cell function, despite their equal expression levels. These results suggest that CAR signaling intensity into T cells was affected not only by CAR expression level, but also by the hinge domain.

A soluble form of the rat CD8 alpha chain was produced by introducing a stop codon into the cDNA at the end of the region encoding the extracellular sequence and expressed in Chinese hamster ovary cells. sCD8 alpha was produced at 20 mg/l, and consisted of monomers, dimers, and higher aggregates.

We have now determined the 2.8 Å resolution crystal structure of a complex containing the murine CD8αα (mCD8αα) homodimer and a murine MHC class I molecule H-2K b loaded with an octapeptide. The latter represents amino acids 52–59 of the vesicular stomatitis virus nuclear capsid protein (VSV8).

Deletion of Gly-Gly in CD8 Hinge Region of CAR Reduced the Flexibility of Hinge Without Affecting the CAR Expression Efficiency. The 2nd CAR-T cells, structured as FMC63-CD8-4-1BB-CD3ζ, have shown promising efficacy in clinical studies .

Mar 13, 2017 · A hinge domain is a structure between the targeting moiety and the T cell plasma membrane ; these sequences are generally derived from IgG subclasses (such as IgG1 and IgG4), IgD and CD8 domains, of which IgG1 has been most extensively used [19–21].

Feb 1, 1992 · The lymphocyte surface CD8 antigen is a heterodimer with each chain containing a single Ig-related domain, a hinge-like sequence, a transmembrane segment, and a short cytoplasmlc sequence.

We outline the unique structure and function of different CD8 domains (ectodomain, hinge, transmembrane, cytoplasmic tail) in the context of the distinct properties of CD8αα homodimers and CD8αβ heterodimers. We discuss CD8 features commonly used to construct chimeric antigen receptors for immunotherapy.

We find that a CD22-targeting CAR harboring a CD8α hinge (H) exhibits greater cytotoxicity against a low antigen density CD22 + leukemia as compared to an equivalent CAR with a CD28 H. We therefore studied the biophysical and dynamic properties of the CD8α H by nuclear magnetic resonance (NMR) spectroscopy.

The lymphocyte surface CD8 antigen is a heterodimer with each chain containing a single Ig-related domain, a hinge-like sequence, a transmembrane segment, and a short cytoplasmic sequence.