Preece Andrew F, Strahan Karen M, Devitt James, Yamamoto Fumi-ichiro, Gustafsson Kenth
Molecular Immunology Unit, Institute of Child Health, University College London, 30 Guilford Street, London WC1N 1EH, United Kingdom.
Blood. 2002 Apr 1;99(7):2477-82. doi: 10.1182/blood.v99.7.2477.
No definitive biologic function has been associated with the human ABO histo-blood group polymorphism, or any other terminal carbohydrate differences within or between closely related species. We have experimentally addressed the question of whether viral particles can become glycosylated as determined by the glycosylation (eg, ABO) status of the producer cell and as a result be affected by human serum containing specific natural antibodies (NAbs). Measles virus was produced in cells transfected with cDNA encoding, either human A-transferase, B-transferase, an inactive "O-transferase," or a pig alpha1-3galactosyltransferase (alpha1-3GT) synthesizing the Galalpha1-3Gal structure. The viruses were shown to carry the same ABO structures as the cells; that is, A but not B if produced in A-type cells, and B but not A if produced in B-type cells. Only O was detected on the virus produced from O-type cells, whereas reduced amounts of O appeared on the A- and B-type viral particles. In addition, the Galalpha1-3Gal structure was transferred onto measles only when grown in human cells expressing this structure. When subjected to human preimmune sera, the A-type, the B-type, and the Galalpha1-3Gal viral particles were partially neutralized in a complement-dependent manner. However, the O-type or the Galalpha1-3Gal-negative viral particles were not neutralized. The neutralization appeared to be mediated by specific NAb, as judged by specific inhibition using synthetic A and Galalpha1-3Gal oligosaccharides. Such viral glycosylation may thus partly explain why the ABO antigens and other similar intraspecies as well as interspecies polymorphic carbohydrates have evolved and been maintained over long evolutionary periods.
人类ABO组织血型多态性或密切相关物种内部或之间的任何其他末端碳水化合物差异均未与明确的生物学功能相关联。我们通过实验探讨了病毒颗粒是否会根据产生细胞的糖基化（例如ABO）状态进行糖基化，并因此受到含有特定天然抗体（NAb）的人血清影响的问题。麻疹病毒是在转染了编码人A转移酶、B转移酶、无活性的“O转移酶”或合成Galα1-3Gal结构的猪α1-3半乳糖基转移酶（α1-3GT）的cDNA的细胞中产生的。结果表明，这些病毒携带的ABO结构与细胞相同；也就是说，在A型细胞中产生的病毒携带A结构而非B结构，在B型细胞中产生的病毒携带B结构而非A结构。在O型细胞产生的病毒上仅检测到O结构，而在A型和B型病毒颗粒上O结构的含量减少。此外，只有在表达该结构的人细胞中生长时，Galα1-3Gal结构才会转移到麻疹病毒上。当用人类免疫前血清处理时，A型、B型和Galα1-3Gal病毒颗粒以补体依赖的方式被部分中和。然而，O型或Galα1-3Gal阴性病毒颗粒未被中和。通过使用合成A和Galα1-3Gal寡糖进行特异性抑制判断，这种中和作用似乎是由特异性NAb介导的。因此，这种病毒糖基化可能部分解释了为什么ABO抗原以及其他类似的种内和种间多态性碳水化合物在漫长的进化过程中得以进化并保留下来。
