C305的产生与特性鉴定，C305是一种可抑制BLyS与其受体BCMA结合的鼠源中和性单链抗体片段（scFv）。

Generation and characterization of C305, a murine neutralizing scFv antibody that can inhibit BLyS binding to its receptor BCMA.

作者信息

Liu Mei-Yun, Han Wei, Ding Yan-Li, Zhou Tian-Hong, Tian Rui-Yang, Yang Sheng-Li, Liu Hui, Gong Yi

机构信息

College of Life Science and Technology, Jinan University, Guangzhou 510632, China.

出版信息

Acta Biochim Biophys Sin (Shanghai). 2005 Jun;37(6):415-20. doi: 10.1111/j.1745-7270.2005.00059.x.

DOI:10.1111/j.1745-7270.2005.00059.x

Abstract

B-lymphocyte stimulator (BLyS) is a member of the tumor necrosis factor (TNF) family and a key regulator of B cell response. Neutralizing single-chain fragment variable (scFv) antibody against BLyS binding to its receptor BCMA has the potential to play a prominent role in autoimmune disease therapy. A phage display scFv library constructed on pIII protein of M13 filamentous phage was screened using BLyS. After five rounds of panning, their binding activity was characterized by phage-ELISA. Nucleotide sequencing revealed that at least two different scFv gene fragments (C305 and D416) were obtained. The two different scFv gene fragments were expressed to obtain the soluble scFv antibodies, then the soluble scFv antibodies were characterized by means of competitive ELISA and in vitro neutralization assay. The results indicated that C305 is the neutralizing scFv antibody that can inhibit BLyS binding to its receptor BCMA.

摘要

B淋巴细胞刺激因子（BLyS）是肿瘤坏死因子（TNF）家族的一员，也是B细胞反应的关键调节因子。针对BLyS与其受体BCMA结合的中和性单链可变片段（scFv）抗体在自身免疫性疾病治疗中可能发挥重要作用。使用BLyS筛选了构建在M13丝状噬菌体pIII蛋白上的噬菌体展示scFv文库。经过五轮淘选后，通过噬菌体酶联免疫吸附测定（phage-ELISA）对它们的结合活性进行了表征。核苷酸测序显示至少获得了两个不同的scFv基因片段（C305和D416）。表达这两个不同的scFv基因片段以获得可溶性scFv抗体，然后通过竞争性酶联免疫吸附测定和体外中和试验对可溶性scFv抗体进行表征。结果表明，C305是能够抑制BLyS与其受体BCMA结合的中和性scFv抗体。