Daviet L, Buckland R, Puente Navazo M D, McGregor J L
INSERM Unit 331, Faculty of Medicine Alexis Carrel, Lyon, France.
Biochem J. 1995 Jan 1;305 ( Pt 1)(Pt 1):221-4. doi: 10.1042/bj3050221.
The human CD36 antigen is a multifunctional membrane glycoprotein that acts as a receptor for thrombospondin, malaria-infected erythrocytes and oxidized low-density lipoprotein, as well as being implicated in the recognition of apoptotic neutrophils by macrophages. OKM5 and other anti-CD36 monoclonal antibodies have been shown to inhibit these CD36 adhesive functions, suggesting that the monoclonal-antibody epitopes and the domains that mediate these events are closely related. Analysis of a series of chimaeric exchanges between human and mouse CD36 shows that six anti-CD36 monoclonal antibodies (OKM5, FA6-152, L103, 5F1, SM phi and 10/5) recognize epitopes within the domain comprising amino acids 155-183. A seventh monoclonal antibody (13/10) binds to another domain that spans amino acids 30-76. Homologue-replacement mutagenesis performed within the human 155-183 immunodominant sequence identifies key residues for the binding of three functional monoclonal antibodies (OKM5, FA6-152 and L103). The fact that antibodies directed against the 155-183 domain can inhibit adhesion suggests that this domain is directly involved in CD36-ligand binding.
人类CD36抗原是一种多功能膜糖蛋白，它作为血小板反应蛋白、疟疾感染的红细胞和氧化型低密度脂蛋白的受体，同时也参与巨噬细胞对凋亡中性粒细胞的识别。OKM5及其他抗CD36单克隆抗体已被证明可抑制这些CD36的黏附功能，这表明单克隆抗体表位与介导这些事件的结构域密切相关。对一系列人源和鼠源CD36之间的嵌合交换进行分析表明，六种抗CD36单克隆抗体（OKM5、FA6-152、L103、5F1、SM phi和10/5）识别包含氨基酸155 - 183的结构域内的表位。第七种单克隆抗体（13/10）则结合到另一个跨越氨基酸30 - 76的结构域。在人源155 - 183免疫显性序列内进行的同源置换诱变确定了三种功能性单克隆抗体（OKM5、FA6-152和L103）结合的关键残基。针对155 - 183结构域的抗体能够抑制黏附这一事实表明，该结构域直接参与CD36与配体的结合。
