摘要: S-layer proteins create a cell-surface layer architecture in both bacteria and archaea. Because S-layer proteins self-assemble into a native-like S-layer crystalline structure in vitro, they are attractive building blocks in nanotechnology. Here, the potential use of the S-layer protein EA1 from Bacillus anthracis in constructing a functional nanostructure is investigated, and apply this nanostructure in a proof-of-principle study for serological diagnosis of anthrax. EA1 is genetically fused with methyl parathion hydrolase (MPH), to degrade methyl parathion and provide a label for signal amplifi cation. EA1 not only serves as a nanocarrier, but also as a specific antigen to capture anthrax-specific antibodies. As results, purified EA1-MPH forms a single layer of crystalline nanostructure through self-assembly. Our chimeric nanocatalyst greatly improves enzymatic stability of MPH. When applied to the detection of anthrax-specific antibodies in serum samples, the detection of our EA1-MPH nanostructure is nearly 300 times more sensitive than that of the unassembled complex. Together, it is shown that it is possible to build a functional and highly sensitive nanosensor based on S-layer protein. In conclusion, our present study should serve as a model for the development of other multifunctional nanomaterials using S-layer proteins.
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期刊:
SMALL
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分类:
生物学
>>
生物物理学
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引用:
ChinaXiv:201605.01440
(或此版本
ChinaXiv:201605.01440V1)
DOI:10.12074/201605.01440V1
CSTR:32003.36.ChinaXiv.201605.01440.V1
- 推荐引用方式:
Wang, Xu-Ying,Wang, Dian-Bing,Bi, Li-Jun,Zhang, Xian-En,Wang, Xu-Ying,Zhang, Ji-Bin,Zhang, Zhi-Ping,Ding, Wei.(2016).A S-Layer Protein of Bacillus anthracis as a Building Block for Functional Protein Arrays by In Vitro Self-Assembly.SMALL.[ChinaXiv:201605.01440]
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