A new member of the immunoglobulin superfamily—CTLA-4

  title={A new member of the immunoglobulin superfamily—CTLA-4},
  author={Jean-François Brunet and François Denizot and Maria Luciani and M Roux-Dosseto and Marie Suzan and Marie Genevi{\`e}ve Mattei and Pierre Golstein},
The immunoglobulin superfamily is a group of proteins, each made of one or several domains sharing key structural features with either the variable (V) or the constant (C) immunoglobulin domains1,2. It includes such functionally important members as the immunoglobulins themselves, major histocompatibility complex (MHC) class I and class II and T-cell receptor (TCR) molecules. Several members of this superfamily are expressed on lymphocytes where they are membrane-bound and capable of… 
Identification of residues in the V domain of CD80 (B7-1) implicated in functional interactions with CD28 and CTLA4
Human CD80 mutants were generated and tested for their ability to maintain the interaction with CD28 leading to adhesion and enhanced IL-2 production, and two hydrophobic residues in the V-like domain of CD80 were identified as critical for binding to CD28 and are also important for the contact with CTLA4.
CTLA4-Ig, a fusion protein, consisting of the extracellular domain of CTLA4 in combination with the constant region of the human immunoglobulin Cy chain, has been developed to investigate the effects of inhibition of the B7/CD28 costimulatory pathway on transplant rejection.
Monoclonal Antibody IOTest ® CD122-PE
CD152 antigen was recently reported to be expressed on human B cells at even higher levels than on activated T cells, when cultured with activated T Cells, using mixed CD2 activating monoclonal antibodies.
Crystal structure of the receptor-binding domain of human B7-2: Insights into organization and signaling
Crystal structure of the receptor-binding (Ig V-type) domain of human B7-2 at 2.7-Å resolution suggests a physical–chemical basis for the observed functional similarities and differences between these two costimulatory ligands.
Cloning of feline cDNA encoding the cytotoxic T lymphocyte-associated antigen 4 (CTLA-4).
The hexapeptide motif (MYPPPY) within the extra-cellular domain of CTLA-4 molecule, which is believed to be responsible for interaction with the B7 family members, is completely conserved in all the species.
Cd28 and Ctla-4, two related members of the Ig supergene family, are tightly linked on proximal mouse chromosome 1
Segregation analysis, using a panel of interspecific backcross mice, indicates that Cd28 is closely linked with Ctla-4 with no recombinations detected in 114 meiotic events examined, which suggests that these two members of the Ig supergene family may be members of a complex of closely related genes similar to other Igsupergene clusters.
CTLA-4 is a second receptor for the B cell activation antigen B7
These findings provide direct evidence that, like its structural homologue CD28, CTLA- 4 is able to bind the B7 counter-receptor on activated B cells.