VISTA.18 binds to the VISTA protein and inhibits its binding to PSGL-1.
Suitable for ELISA, SPR, FuncS, Co-crystallization
Isotype: IgG
Various conjugated forms available upon request.
Summary
Specifications
Antibody Isotype
IgG
Clone
VISTA.18
Species Reactivity
Human
Immunogen
Recombinant human VISTA
Conjugate
Unconjugated
Applications
Application Notes
ELISA, SPR, FuncS, Co-crystallization Each laboratory should determine an optimum working titer for use in its particular application. Other applications have not been tested but use in such assays should not necessarily be excluded.
General Notes
VISTA.18 binds to VISTA and blocks its binding to P-selectin glycoprotein ligand 1 (PSGL-1). VISTA is a protein that acts as both a ligand and a receptor. It binds to PSGL-1 and V-set and Ig domain-containing 3 (VSIG3) ligands, which are both immunosuppressive. VISTA's binding to these ligands inhibits T cell function.
Target
Alternative Names
V-type immunoglobulin domain-containing suppressor of T cell activation; V-domain Ig suppressor of T cell activation; VISTA
Citations
Publication ()
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References
VISTA is an acidic pH-selective ligand for PSGL-1.
Co-inhibitory immune receptors can contribute to T cell dysfunction in patients with cancer 1,2 . Blocking antibodies against cytotoxic T-lymphocyte-associated protein 4 (CTLA-4) and programmed cell death 1 (PD-1) partially reverse this effect and are becoming standard of care in an increasing number of malignancies 3 . However, many of the other axes by which tumours become inhospitable to T cells are not fully understood. Here we report that V-domain immunoglobulin suppressor of T cell activation (VISTA) engages and suppresses T cells selectively at acidic pH such as that found in tumour microenvironments. Multiple histidine residues along the rim of the VISTA extracellular domain mediate binding to the adhesion and co-inhibitory receptor P-selectin glycoprotein ligand-1 (PSGL-1). Antibodies engineered to selectively bind and block this interaction in acidic environments were sufficient to reverse VISTA-mediated immune suppression in vivo. These findings identify a mechanism by which VISTA may engender resistance to anti-tumour immune responses, as well as an unexpectedly determinative role for pH in immune co-receptor engagement.