Application of the bacterial C-DAG system to analyze the ability of amyloids to seed protein aggregation in vitro

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The search for new amyloid proteins, as well as the study of their properties, is an actual task, which can be solved by a number of different model systems. One of the most popular is the C-DAG approach. It is based on the analysis of aggregation of the investigated proteins on the surface of Escherichia coli cells. According to the original protocol, it can be used to demonstrate one of the characteristic properties of amyloids: the ability to bind the amyloid-specific dye Congo red and demonstrate apple-green birefringence. In addition, the C-DAG technique allows one to analyze the morphology of aggregates and their resistance to detergents. In this work, we tested using Sup35NM as an example whether aggregates on the surface of bacterial cells can act as inducers of aggregation of the corresponding protein.

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作者简介

N. Trubitsina

Saint Petersburg State University

Email: s.bondarev@spbu.ru

Department of Genetics and Biotechnology

俄罗斯联邦, 1199034, Saint Petersburg

O. Zemlyanko

Saint Petersburg State University

Email: stanislavspbgu@gmail.com

Department of Genetics and Biotechnology, Laboratory of Amyloid Biology

俄罗斯联邦, 1199034, Saint Petersburg

G. Zhouravleva

Saint Petersburg State University

Email: s.bondarev@spbu.ru

Department of Genetics and Biotechnology, Laboratory of Amyloid Biology

俄罗斯联邦, 1199034, Saint Petersburg

S. Bondarev

Saint Petersburg State University

编辑信件的主要联系方式.
Email: stanislavspbgu@gmail.com

Department of Genetics and Biotechnology, Laboratory of Amyloid Biology

俄罗斯联邦, 1199034, Saint Petersburg

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2. Figure. Bacterial cells with Sup35NM fibrils accelerate the aggregation of Sup35NM protein in vitro. ∅ ‒ spontaneous aggregation of Sup35NM. “NS” ‒ no significant differences; * ‒ p-value < 0.05 (Wilcoxon test).

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