Self-assembly of Aeropyrum pernix bacilliform virus 1 (APBV1) major capsid protein and its application as building blocks for nanomaterials.

IF 4.6 Q2 MATERIALS SCIENCE, BIOMATERIALS

ACS Applied Bio Materials Pub Date : 2022-11-13 DOI:10.1007/s00792-022-01284-x

Yuka Sumikama, Atsushi Takashima, Tomohiro Mochizuki, Haruhiko Sakuraba, Toshihisa Ohshima, Shinji Sugihara, Shin-Ichiro Suye, Takenori Satomura

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Abstract

Virus capsid proteins have various applications in diverse fields such as biotechnology, electronics, and medicine. In this study, the major capsid protein of bacilliform clavavitus APBV1, which infects the hyperthermophilic archaeon Aeropyrum pernix, was successfully expressed in Escherichia coli. The gene product was expressed as a histidine-tagged protein in E. coli and purified to homogeneity using single-step nickel affinity chromatography. The purified recombinant protein self-assembled to form bacilliform virus-like particles at room temperature. The particles exhibited tolerance against high concentrations of organic solvents and protein denaturants. In addition, we succeeded in fabricating functional nanoparticles with amine functional groups on the surface of ORF6-81 nanoparticles. These robust protein nanoparticles can potentially be used as a scaffold in nanotechnological applications.

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沼草杆菌状病毒1 (APBV1)主要衣壳蛋白的自组装及其在纳米材料构建中的应用

病毒衣壳蛋白在生物技术、电子、医学等领域有着广泛的应用。本研究成功地在大肠杆菌中表达了侵染嗜热太古菌Aeropyrum pernix的棒状芽孢杆菌(bacillform clavavitus)主要衣壳蛋白APBV1。该基因产物在大肠杆菌中以组氨酸标记蛋白的形式表达，并通过镍亲和层析法纯化。纯化后的重组蛋白在室温下自组装形成杆菌状病毒样颗粒。颗粒对高浓度有机溶剂和蛋白质变性剂表现出耐受性。此外，我们成功地在ORF6-81纳米颗粒表面制备了具有胺官能团的功能纳米颗粒。这些坚固的蛋白质纳米颗粒可以潜在地用作纳米技术应用中的支架。

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来源期刊

ACS Applied Bio Materials Chemistry-Chemistry (all)

CiteScore

9.40

自引率

2.10%

发文量

464