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Poly-protein G-expressing bacteria enhance the sensitivity of immunoassays.
Hao, Wen-Rui; Chen, Michael; Chen, Yi-Jou; Su, Yu-Cheng; Cheng, Chiu-Min; Hsueh, Hsiang-Yin; Kao, An-Pei; Hsieh, Yuan-Chin; Chang, Johny; Tseng, Ming-Yang; Chuang, Kuo-Hsiang.
Afiliación
  • Hao WR; Division of Cardiovascular Medicine, Department of Internal Medicine, Shuang Ho Hospital, Taipei Medical University, New Taipei City, Taiwan.
  • Chen M; Ph.D. program for the Clinical Drug Discovery from Botanical Herbs, Taipei Medical University, Taipei, Taiwan.
  • Chen YJ; Ph.D. program for the Clinical Drug Discovery from Botanical Herbs, Taipei Medical University, Taipei, Taiwan.
  • Su YC; Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan.
  • Cheng CM; Department of Aquaculture, National Kaohsiung Marine University, Kaohsiung, Taiwan.
  • Hsueh HY; School of Pharmacy, Taipei Medical University, Taipei, Taiwan.
  • Kao AP; Stemforce Biotechnology Co., Ltd, Chiayi City, Taiwan.
  • Hsieh YC; Graduate Institute of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
  • Chang J; Graduate Institute of Pharmacognosy, Taipei Medical University, Taipei, Taiwan.
  • Tseng MY; Graduate Institute of Medicine, Kaohsiung Medical University, Kaohsiung, Taiwan.
  • Chuang KH; Ph.D. program for the Clinical Drug Discovery from Botanical Herbs, Taipei Medical University, Taipei, Taiwan. khchuang@tmu.edu.tw.
Sci Rep ; 7(1): 989, 2017 04 20.
Article en En | MEDLINE | ID: mdl-28428542
The sensitivities of solid-phase immunoassays are limited by the quantity of detection antibodies bound to their antigens on the solid phase. Here, we developed a poly-protein G-expressing bacterium as an antibody-trapping microparticle to enhance the signals of immunoassays by increasing the accumulation of detection antibodies on the given antigen. Eight tandemly repeated fragment crystallisable (Fc) binding domains of protein G were stably expressed on the surface of Escherichia coli BL21 cells (termed BL21/8G). BL21/8G cells showed a higher avidity for trapping antibodies on their surface than monomeric protein G-expressing BL21 (BL21/1G) cells did. In the sandwich enzyme-linked immunosorbent assay (ELISA), simply mixing the detection antibody with BL21/8G provided a detection limit of 6 pg/mL for human interferon-α (IFN-α) and a limit of 30 pg/mL for polyethylene glycol (PEG)-conjugated IFN-α (Pegasys), which are better than that of the traditional ELISA (30 pg/mL for IFN-α and 100 pg/mL for Pegasys). Moreover, the sensitivity of the Western blot for low-abundance Pegasys (0.4 ng/well) was increased by 25 folds upon mixing of an anti-PEG antibody with BL21/8G cells. By simply being mixed with a detection antibody, the poly-protein G-expressing bacteria can provide a new method to sensitively detect low-abundance target molecules in solid-phase immunoassays.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Escherichia coli / Anticuerpos Monoclonales / Antígenos Bacterianos Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Sci Rep Año: 2017 Tipo del documento: Article País de afiliación: Taiwán Pais de publicación: Reino Unido

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Escherichia coli / Anticuerpos Monoclonales / Antígenos Bacterianos Tipo de estudio: Diagnostic_studies Límite: Humans Idioma: En Revista: Sci Rep Año: 2017 Tipo del documento: Article País de afiliación: Taiwán Pais de publicación: Reino Unido