Tahiri Fatima, Li Yunsen, Hawke David, Ganiko Luciane, Almeida Igor, Levery Steven, Zhou Dapeng
MD Anderson Cancer Center, University of Texas, Houston, Texas, USA.
J Carbohydr Chem. 2013 Jan 1;32(1):44-67. doi: 10.1080/07328303.2012.741637. Epub 2013 Jan 11.
α-1,3-Terminated galactose residues on glycoproteins and glycosphingolipids are recognized by natural anti-α-1,3-galactose antibodies in human serum and cause hyperacute rejection in pig-to-human xenotransplantation. Genetic depletion of α-1,3-galactosyltransferase-1 in pigs abolishes the hyperacute rejection reaction. However, the isoglobotriosylceramide (iGb3) synthase in pigs may produce additional α-1,3-terminated galactose residues on glycosphingolipids. In both α-1,3-galactosyltranserase-1 knockout mice and pigs, cytotoxic anti-α-1,3-galactose antibodies could be induced; thus, a paradox exists that anti-α-1,3-galactose antibodies are present in animals with functional iGb3 synthases. Furthermore, iGb3 has been found to be an endogenous antigen for natural killer T (NKT) cells, an innate type of lymphocyte that may initiate the adaptive immune responses. It has been reasoned that iGb3 may trigger the activation of NKT cells and cause the rejection of α-1,3-galactosyltransferase-1-deficient organs through the potent stimulatory effects of NKT cells on adaptive immune cells (see ref.([20])). In this study, we examined the expression of iGb3 and the isoglobo-series glycosphingolipids in pig organs, including the heart, liver, pancreas, and kidney, by ion-trap mass spectrometry, which has a sensitivity of measuring 1% iGb3 among Gb3 isomers, when 5 μg/mL of the total iGb3/Gb3 mixture is present (see ref.([35])). We did not detect iGb3 or other isoglobo-series glycosphingolipids in any of these organs, although they were readily detected in mouse and human thymus and dendritic cells. The lack of iGb3 and isoglobo-series glycosphingolipids in pig organs indicates that iGb3 is unlikely to be a relevant immune epitope in xenotransplantation.
糖蛋白和糖鞘脂上的α-1,3-末端半乳糖残基可被人血清中的天然抗α-1,3-半乳糖抗体识别,并在猪到人的异种移植中引发超急性排斥反应。猪体内α-1,3-半乳糖基转移酶-1的基因缺失消除了超急性排斥反应。然而,猪体内的异球三糖神经酰胺(iGb3)合酶可能会在糖鞘脂上产生额外的α-1,3-末端半乳糖残基。在α-1,3-半乳糖基转移酶-1基因敲除小鼠和猪中,均可诱导产生细胞毒性抗α-1,3-半乳糖抗体;因此,存在一个悖论,即具有功能性iGb3合酶的动物体内存在抗α-1,3-半乳糖抗体。此外,iGb3已被发现是自然杀伤T(NKT)细胞的内源性抗原,NKT细胞是一种先天性淋巴细胞,可能启动适应性免疫反应。据推测,iGb3可能通过NKT细胞对适应性免疫细胞的强大刺激作用触发NKT细胞的激活,并导致对α-1,3-半乳糖基转移酶-1缺陷器官的排斥(见参考文献[20])。在本研究中,我们通过离子阱质谱法检测了猪器官(包括心脏、肝脏、胰腺和肾脏)中iGb3和异球系列糖鞘脂的表达,当存在5μg/mL的总iGb3/Gb3混合物时,该方法测量Gb3异构体中1%的iGb3的灵敏度(见参考文献[35])。我们在这些器官中均未检测到iGb3或其他异球系列糖鞘脂,尽管它们在小鼠和人类胸腺及树突状细胞中很容易被检测到。猪器官中缺乏iGb3和异球系列糖鞘脂表明iGb3不太可能是异种移植中相关的免疫表位。