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Evaluation of intermolecular forces between lipopolysaccharides and monoclonal antibodies using atomic force microscopy.

作者信息

Ananchenko Boris, Belozerov Vladislav, Byvalov Andrey, Konyshev Ilya, Korzhavina Anastasia, Dudina Lyubov

机构信息

Vyatka State University, Kirov 610000, Russian Federation.

The Institute of Physiology of the Коmi Science Centre of the Ural Branch of the Russian Academy of Sciences, FRC Komi SC UB RAS, Syktyvkar, Komi Republic 167982, Russian Federation; Vyatka State University, Kirov 610000, Russian Federation.

出版信息

Int J Biol Macromol. 2020 Aug 1;156:841-850. doi: 10.1016/j.ijbiomac.2020.04.055. Epub 2020 Apr 17.

DOI:10.1016/j.ijbiomac.2020.04.055
PMID:32305368
Abstract

Understanding of interactions between a bacterium and an immune or non-immune host organism at the cellular and subcellular level is important in order to improve new and existing immunobiological tools for the treatment of bacterial infections (including pseudotuberculosis). The aim of this work was to quantify the interaction force between Yersinia pseudotuberculosis and monoclonal antibodies (mAbs) in the model system "lipopolysaccharide (LPS) - mAbs" by atomic force microscopy (AFM). Our research findings provided the methodical approaches to force measurements between an AFM probe, which was functionalized with Y. pseudotuberculosis LPS, and mica coated by different mAbs. Based on the criteria for force estimation there was shown a greater binding force in the system "LPS - complementary mAbs" than in the system "LPS - heterologous mAbs". In both cases binding force increase followed by increase a contact time between the functionalized AFM probe and mica from 1 to 5 s. It has been shown that single bonds between LPS and complementary mAbs molecules also included a clearly defined non-specific component along with immunochemically specific one. The evidence suggests a significant proportion of applied force exerted to unfolding of high-molecular aggregates whose length may attain many hundreds of nanometers.

摘要

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引用本文的文献

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Single-Molecule-Level Quantification Based on Atomic Force Microscopy Data Reveals the Interaction between Melittin and Lipopolysaccharide in Gram-Negative Bacteria.基于原子力显微镜数据的单分子水平定量分析揭示了蜂毒素与革兰氏阴性菌中脂多糖的相互作用。
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