Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran.
Biotechnology Research Centre, Venom and Biotherapeutics Molecules Laboratory, Pasteur Institute of Iran, Tehran, 1316543551, Iran.
Mol Biotechnol. 2023 Dec;65(12):1968-1978. doi: 10.1007/s12033-023-00700-7. Epub 2023 Mar 11.
As a member of the tumor necrosis factor (TNF) superfamily, the B-cell activating factor (BAFF) plays a crucial role in B-cell survival and differentiation. Overexpression of this protein has been closely linked to autoimmune disorders and some B-cell malignancies. Using monoclonal antibodies (mAbs) against the BAFF soluble domain appears to be a complementary treatment for some of these diseases. This study aimed to produce and develop a specific Nanobody (Nb), a variable camelid antibody domain, against the soluble domain of BAFF protein. After camel immunization with recombinant protein and preparing cDNA from total RNAs separated from camel lymphocytes, an Nb library was developed. Individual colonies capable of binding selectively to rBAFF were obtained by periplasmic-ELISA, sequenced, and expressed in a bacterial expression system. The specificity and affinity of selected Nb were determined and its target identification and functionality were evaluated using flow cytometry.
作为肿瘤坏死因子 (TNF) 超家族的一员,B 细胞激活因子 (BAFF) 在 B 细胞存活和分化中发挥着关键作用。这种蛋白的过度表达与自身免疫性疾病和一些 B 细胞恶性肿瘤密切相关。使用针对 BAFF 可溶性结构域的单克隆抗体 (mAb) 似乎是治疗这些疾病的一种补充方法。本研究旨在制备和开发针对 BAFF 蛋白可溶性结构域的特异性纳米抗体 (Nb),一种可变的骆驼科抗体结构域。骆驼经重组蛋白免疫后,从骆驼淋巴细胞分离的总 RNA 中制备 cDNA,然后开发 Nb 文库。通过周质内 ELISA 获得能够选择性结合 rBAFF 的单个菌落,对其进行测序,并在细菌表达系统中表达。通过流式细胞术测定选定 Nb 的特异性和亲和力,并评估其靶标鉴定和功能。