Rojo S, Wagtmann N, Long E O
Laboratory of Immunogenetics, National Institute of Allergy and Infectious Diseases, Rockville, MD 20852-1727, USA.
Eur J Immunol. 1997 Feb;27(2):568-71. doi: 10.1002/eji.1830270231.
Lysis of target cells by natural killer (NK) cells can be prevented by killer cell inhibitory receptors (KIR) specific for major histocompatibility complex class I molecules. Functional studies have identified two distinct p58 KIR, each reactive with a different group of HLA-C allotypes, and distinct p70 KIR specific for some HLA-B or HLA-A allotypes. The NK specificities for each group of HLA-C allotypes have been reproduced by direct binding of recombinant soluble p58 molecules. Here, we show that a soluble p70 KIR binds to HLA-B5101, but not to HLA-A or HLA-C molecules. Truncated soluble forms of the HLA-B5101-specific p70 KIR, including one with two immunoglobulin (Ig) domains reactive with a monoclonal antibody that blocks p70 KIR function, did not bind to HLA-B*5101, indicating that all three Ig domains are required for binding.
自然杀伤（NK）细胞对靶细胞的裂解可被主要组织相容性复合体I类分子特异性的杀伤细胞抑制受体（KIR）所阻止。功能研究已鉴定出两种不同的p58 KIR，每种都与不同组的HLA - C同种异型反应，以及对某些HLA - B或HLA - A同种异型特异的不同p70 KIR。通过重组可溶性p58分子的直接结合，已重现了每组HLA - C同种异型的NK特异性。在此，我们表明可溶性p70 KIR与HLA - B5101结合，但不与HLA - A或HLA - C分子结合。HLA - B5101特异性p70 KIR的截短可溶性形式，包括一种带有两个免疫球蛋白（Ig）结构域且与阻断p70 KIR功能的单克隆抗体反应的形式，不与HLA - B*5101结合，表明结合需要所有三个Ig结构域。
