| First Author | Carayannopoulos LN | Year | 2002 |
| Journal | Eur J Immunol | Volume | 32 |
| Issue | 3 | Pages | 597-605 |
| PubMed ID | 11857333 | Mgi Jnum | J:187951 |
| Mgi Id | MGI:5438769 | Doi | 10.1002/1521-4141(200203)32:3<597::aid-immu597>3.3.co;2-5 |
| Citation | Carayannopoulos LN, et al. (2002) Ligands for murine NKG2D display heterogeneous binding behavior. Eur J Immunol 32(3):597-605 |
| abstractText | NKG2D transmits stimulatory signals to natural killer cells and other hematopoietic cells, leading to enhanced proliferation, cytokine secretion and target killing. Murine and human NKG2D each recognize five known class I-related molecules with distinct primary structures. Here, we used surface plasmon resonance to examine the binding of murine NKG2D to its cognate ligands: RAE-1B6 (a newly described C57BL/6J variant of RAE-1), RAE-1 delta (common to BALB and C57BL6/J), and H60 (expressed in BALB, but not C57BL/6J). While RAE-1B6 and H60 display relatively high affinities for NKG2D with K(D) in the 20-30 nM range and k(off )in the 0.03s(-1) to 0.06s(-1) range (t(1/2) approximately 10-20s); the RAE-1 delta variant binds with a lower affinity: K(D) of approximately 750 nM. Furthermore, RAE-1 delta displays biphasic kinetics with dominant k(off) of approximately 0.2s(-1) (t(1/2) approximately 3s), partially explaining the lower affinity. Thus, H60 and RAE-1B6 bind NKG2D with almost identical kinetics while sharing only 20% amino acid sequence identity; whereas other RAE-1 molecules demonstrate faster dissociation and lower affinities than RAE-1B6 despite sharing 90% sequence identity. C57BL/6J mice, although not expressing the H60 gene product, retain a high-affinity ligand for NKG2D in the form of RAE-1B6. |
