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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Molecular cloning and biological characterization of NK cell activation-inducing ligand, a counterstructure for CD48.

Using the monoclonal antibody C1.7, which recognizes a signaling, membrane-bound molecule on human NK and a proportion of CD8(+) T cells, we cloned a novel molecule we refer to as NK cell activation-inducing ligand (NAIL). It is a 365-amino acid protein that belongs to the immunoglobulin-like superfamily with closest homology to murine 2B4, and human CD84 and CD48. Using a soluble NAIL-Fc fusion protein, we determined the counterstructure for NAIL, CD48, which it binds with high affinity. Stimulation of human B cells with recombinant NAIL in the presence of a suboptimal concentration of human CD40 ligand or IL-4 resulted in increased proliferation. Treatment of human dendritic cells with soluble NAIL-leucine zipper protein resulted in an increased release of IL-12 and TNF-alpha. Using recombinant CD48 protein, we demonstrated the ability of this molecule to increase NK cell cytotoxicity and induce IFN-gamma production. We also showed that 2B4 binds to mouse CD48, suggesting that interaction of these receptors may play a similar role in both species. Taken together these results indicate that the NAIL-CD48 interaction may be an important mechanism regulating a variety of immune responses.[1]

References

  1. Molecular cloning and biological characterization of NK cell activation-inducing ligand, a counterstructure for CD48. Kubin, M.Z., Parshley, D.L., Din, W., Waugh, J.Y., Davis-Smith, T., Smith, C.A., Macduff, B.M., Armitage, R.J., Chin, W., Cassiano, L., Borges, L., Petersen, M., Trinchieri, G., Goodwin, R.G. Eur. J. Immunol. (1999) [Pubmed]
 
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