Nimmerjahn Falk, Ravetch Jeffrey V
Laboratory of Molecular Genetics and Immunology, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Curr Opin Immunol. 2007 Apr;19(2):239-45. doi: 10.1016/j.coi.2007.01.005. Epub 2007 Feb 8.
Since the first report of the successful use of a monoclonal antibody for the treatment of human B cell lymphoma in 1982, several antibodies have become incorporated into standard treatment protocols for cancer. One of the most important factors that determine antibody activity in vivo is the efficient interaction with cellular Fc-receptors on innate immune effector cells. It has become clear that the outcome of this interaction is influenced by several factors, such as the antibody isotype-specific affinity to activating and inhibitory receptors, the level of inhibitory FcgammaRIIB expression, and the composition of the sugar side chain attached to the antibody Fc-portion. These novel insights into antibody FcR interactions might be useful to produce the next generation of improved immunotherapeutic molecules.
自1982年首次报道成功使用单克隆抗体治疗人类B细胞淋巴瘤以来,已有多种抗体被纳入癌症的标准治疗方案。决定抗体体内活性的最重要因素之一是与天然免疫效应细胞上的细胞Fc受体的有效相互作用。已经清楚的是,这种相互作用的结果受多种因素影响,例如抗体同种型对激活和抑制受体的特异性亲和力、抑制性FcγRIIB的表达水平以及连接到抗体Fc部分的糖侧链的组成。这些关于抗体FcR相互作用的新见解可能有助于生产下一代改良的免疫治疗分子。