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Related Experiment Video

Updated: Jun 9, 2026

Mycobacterium tuberculosis Extracellular Vesicle Enrichment through Size Exclusion Chromatography
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[Expression, purification, and characterization Mycobacterium tuberculosis Rv1168c].

Xiaoli Yu1, Zhanqiang Sun, Chenjun Zhou

  • 1School of Biolgy and Pharmaceutical Engineering, Wuhan Polytechnic University, Wuhan 430023, China. yxll268@126.com

Wei Sheng Wu Xue Bao = Acta Microbiologica Sinica
|September 7, 2010
PubMed
Summary

Researchers successfully expressed and purified the Pro-Pro-Glu (PPE) family protein Rv1168c from Mycobacterium tuberculosis in E. coli. This study provides purified recombinant Rv1168c protein for further functional and structural analysis in tuberculosis research.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • The Pro-Pro-Glu (PPE) family protein Rv1168c is a component of Mycobacterium tuberculosis.
  • Understanding the structure and function of Rv1168c is crucial for tuberculosis research.

Purpose of the Study:

  • To express and purify the Rv1168c protein from Mycobacterium tuberculosis in E. coli.
  • To investigate the secondary and three-dimensional structure of Rv1168c.

Main Methods:

  • Amplification and cloning of the Rv1168c gene into a pET32a prokaryotic expression vector.
  • High-level expression of recombinant Rv1168c in E. coli BL21(DE3) induced by Isopropyl-beta-D-thiogalactopyranoside (IPTG).
  • Analysis of protein molecular weight by SDS-PAGE and mass spectrometry.
  • Determination of secondary and 3D structures using circular dichroism and homologous modeling.

Main Results:

  • Successfully obtained the Mycobacterium tuberculosis Rv1168c gene (971bp) and highly purified recombinant Rv1168c protein.
  • The relative molecular weight of the recombinant Rv1168c protein (including the vector) was determined to be 51.5 kDa.
  • Secondary structure analysis revealed approximately 34.4% alpha helix, 33.7% beta-sheet, and 31.9% random coil at 25°C.
  • Homologous modeling predicted Rv1168c to be a (beta/alpha)5 protein.

Conclusions:

  • Purified recombinant Rv1168c protein was successfully obtained.
  • This study provides a foundation for further investigation into the structure-function relationship of Rv1168c in the context of tuberculosis.