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首页> 外文期刊>Journal of Molecular Biology >Specific recognition of a DNA immunogen by its elicited antibody.
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Specific recognition of a DNA immunogen by its elicited antibody.

机译：DNA免疫原通过其引发的抗体的特异性识别。

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DNA recognition by antibodies is a key feature of autoimmune diseases, yet model systems with structural information are very limited. The monoclonal antibody ED-10 recognizes one of the strands of the DNA duplex used in the immunogenic complex. Modifications of the 5' end decrease the binding affinity and short oligonucleotides retain high binding affinity. We determined crystal structures for the Fab bound to a 6-mer oligonucleotide containing the specific sequence that raised the antibody and compared it with the unliganded Fab. Only the first two bases from the 5' end (dTdC) display electron density and we observe four key hydrogen bonds at the interface. The thymine ring is stacked between TrpH50 and TrpH95, and the cytosine ring is packed against TyrL32. Upon DNA binding, TyrH97 and TrpH95 rearrange to allow subnanomolar binding affinity, five orders of magnitude higher than other reported complexes, possibly because of having gone through affinity maturation. This structure represents the first bona fide antibody DNA immunogen complex described in atomic detail.
机译：抗体对DNA的识别是自身免疫性疾病的关键特征，但是具有结构信息的模型系统非常有限。单克隆抗体ED-10识别免疫原性复合物中使用的DNA双链体的一条链。 5'末端的修饰降低了结合亲和力，短的寡核苷酸保留了高结合亲和力。我们确定了与六聚体寡核苷酸结合的Fab的晶体结构，该寡聚核苷酸包含产生抗体的特定序列，并将其与未结合的Fab进行了比较。仅从5'端（dTdC）的前两个碱基显示电子密度，我们在界面处观察到四个关键氢键。胸腺嘧啶环堆叠在TrpH50和TrpH95之间，胞嘧啶环紧靠TyrL32。 DNA结合后，TyrH97和TrpH95重新排列以允许亚纳摩尔结合亲和力，比其他报道的复合物高五个数量级，这可能是由于经历了亲和力成熟。该结构代表原子详细描述的第一个真正的抗体DNA免疫原复合物。

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