Anti-idiotypic nanobody as citrinin mimotope from a naive alpaca heavy chain single domain antibody library

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• 作者：Yang Xu ; Liang Xiong ; Yanping Li ; Yonghua Xiong…
• 关键词：Anti ; idiotypic antibody ; Citrinin ; Single domain antibody ; Hapten mimicry ; Phage displayed library
• 刊名：Analytical and Bioanalytical Chemistry
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：407
• 期：18
• 页码：5333-5341
• 全文大小：813 KB
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• 作者单位：Yang Xu (1)
  Liang Xiong (1) (2)
  Yanping Li (1)
  Yonghua Xiong (1)
  Zhui Tu (1)
  Jinheng Fu (1)
  Bo Chen (1)
  
  1. State Key Laboratory of Food Science and Technology, Sino-German Joint Research Institute, Nanchang University, Number 235 Nanjing East Road, Nanchang, 330047, Jiangxi, China
  2. Department of Preventive Medicine, Gannan Medical College, Number 1 Yixueyuan Road, Ganzhou, 341000, Jiangxi, China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Analytical Chemistry
  Food Science
  Inorganic Chemistry
  Physical Chemistry
  Monitoring, Environmental Analysis and Environmental Ecotoxicology
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1618-2650

文摘

Compared with peptide-based mimotope, anti-idiotypic antibodies (AIds) are considered as promising biosynthetic surrogate antigen because these antibodies display stable protein conformation. Nevertheless, conventional AIds are generated by immunizing animals with heterologous idiotypic antibody in vivo; isolated AIds commonly exhibit a higher affinity to primary antibodies than target analytes because AIds undergo?an affinity-matured process during immune responses, resulting in low sensitivity in competitive immunoassay. In the present study, an anti-citrinin monoclonal antibody (anti-CIT McAb) was designed as primary antibody; one β-type AI alpaca heavy chain single domain antibody (β-AI VHH) was selected as a citrinin (CIT) surrogate from a naive phage-displayed VHH library. The affinity constant (K D) of obtained β-AI VHH to anti-CIT McAb (160 nM) is 2.35 times lower than that of CIT and ovalbumin conjugates (CIT-OVA) to anti-CIT McAb (68 nM). The developed VHH-based enzyme-linked immunosorbent assay (V-ELISA) can be used to perform dynamic linear detection of CIT in 10?% (v/v) methanol/PBS from 5.0 to 300.0?ng/mL, with a median inhibitory concentration (IC50) of 44.6?ng/mL (n--); this result was twice as good as that of indirect competitive ELISA (ic-ELISA, IC50--6.2?ng/mL) with CIT-OVA as a coating antigen. Moreover, the precision of V-ELISA was evaluated by analyzing average recoveries and coefficient of variations of CIT-spiked cereal sample; the reliability of V-ELISA was also validated with a conventional ic-ELISA. In summary, the proposed strategy has a great potential for panning other β-AI VHH toward small organic molecules from a naive VHH library.