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[来自的Rv3432c的原核表达及生物信息学分析] （原文中“From”后面似乎缺少内容）

[Prokaryotic Expression and Bioinformatic Analysis of Rv3432c From ].

作者信息

Yi Haibo, Gao Xinghong, Luo Guo, Xu Peng, Wang Huan

机构信息

（ 563099） Key Laboratory of Infectious Disease & Bio-safety, Provincial Department of Education, Zunyi Medical University, Zunyi 563099, China.

出版信息

Sichuan Da Xue Xue Bao Yi Xue Ban. 2024 Mar 20;55(2):330-336. doi: 10.12182/20240360401.

DOI:10.12182/20240360401
PMID:38645872
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11026876/
Abstract

OBJECTIVE

To express the protein enconded by the 3432 gene of (.) by prokaryotic expression, to analyze the structure of the Rv3432c protein by using bioinformatics software, and to explore for new drug targets against ..

METHODS

The 3432 gene was amplified by PCR using the genomic DNA of the inactivated . strain H37Rv as the template and a recombinant plasmid was constructed with the expression vector pET-28a. The expression products were analyzed by SDS-PAGE and purified using affinity chromatography. The biological properties of Rv3432c were analyzed with Protparam, the Pfam online tool, SOMPA, Protscale, TMHMM Signalp 6.0, NetPhos3.1, SUMOsp 2.0, and SWISS-MODEL.

RESULTS

pET-28a-3432 recombinant plasmid sequencing results were fully consistent with those of the target gene. SDS-PAGE analysis showed that the fusion protein existed in the form of a soluble protein with a relative molecular mass of about 55×10, which matched the expected size. ProtParam analysis showed that the Rv3432c protein was hydrophilic (showing a GRAVY value of －0.079). Rv3432c was a protein with no transmembrane structural domains or signal peptide. The secondary structure of Rv3432c mainly consisted of random coils (39.78%) and α-helix (39.57%) and was relatively loosely structured.

CONCLUSION

We successfully constructed a prokaryotic expression plasmid of the Rv3432c protein and analyzed its structure using bioinformatics, laying the foundation for further research on the role of Rv3432c in the pathogenesis and progression of tuberculosis as well as the identification of new drug targets against ..

摘要

目的

通过原核表达来表达（.）3432基因编码的蛋白质，利用生物信息学软件分析Rv3432c蛋白的结构，并探索针对..的新药物靶点。

方法

以灭活的.菌株H37Rv的基因组DNA为模板，通过PCR扩增3432基因，并与表达载体pET - 28a构建重组质粒。通过SDS - PAGE分析表达产物，并用亲和层析法进行纯化。使用Protparam、在线工具Pfam、SOMPA、Protscale、TMHMM Signalp 6.0、NetPhos3.1、SUMOsp 2.0和SWISS - MODEL分析Rv3432c的生物学特性。

结果

pET - 28a - 3432重组质粒测序结果与目标基因完全一致。SDS - PAGE分析表明，融合蛋白以可溶性蛋白形式存在，相对分子质量约为55×10，与预期大小相符。ProtParam分析表明，Rv3432c蛋白具有亲水性（GRAVY值为－0.079）。Rv3432c是一种没有跨膜结构域或信号肽的蛋白。Rv3432c的二级结构主要由无规卷曲（39.78%）和α - 螺旋（39.57%）组成，结构相对松散。

结论

我们成功构建了Rv3432c蛋白的原核表达质粒，并利用生物信息学分析了其结构，为进一步研究Rv3432c在结核病发病机制和进展中的作用以及鉴定针对..的新药物靶点奠定了基础。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/ea0ccdad75eb/scdxxbyxb-55-2-330-10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/e29dc21e27f6/scdxxbyxb-55-2-330-1.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/f34596752042/scdxxbyxb-55-2-330-8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/b6889c97b0d2/scdxxbyxb-55-2-330-9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/ea0ccdad75eb/scdxxbyxb-55-2-330-10.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/e29dc21e27f6/scdxxbyxb-55-2-330-1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/afcf8956f5bb/scdxxbyxb-55-2-330-2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/73d1ed9296b0/scdxxbyxb-55-2-330-3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/4543371ed992/scdxxbyxb-55-2-330-4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/050ea671c0f7/scdxxbyxb-55-2-330-5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/4c86d2fcd3ee/scdxxbyxb-55-2-330-6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/f37871a03d42/scdxxbyxb-55-2-330-7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/f34596752042/scdxxbyxb-55-2-330-8.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/b6889c97b0d2/scdxxbyxb-55-2-330-9.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c0b5/11026876/ea0ccdad75eb/scdxxbyxb-55-2-330-10.jpg

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