High level soluble expression, one-step purification and characterization of HIV-1 p24 protein
2011

High Level Expression and Purification of HIV-1 p24 Protein

Sample size: 90 publication Evidence: high

Author Information

Author(s): Zhang Baozhong, Liu Dabin, Bao Zuoyi, Chen Bin, Li Cun, Jiang Huanhuan, Wang Xiaona, Mi Zhiqiang, An Xiaoping, Lu Jun, Tong Yigang

Primary Institution: State Key Laboratory of Pathogen and Biosecurity, Beijing Institute of Microbiology and Epidemiology, Beijing, China

Hypothesis

The study aims to express and purify the p24 protein in soluble form in E. coli.

Conclusion

The soluble recombinant p24 protein specifically reacts with HIV infected sera and elicits HIV p24 specific antibodies in mice, indicating its potential as a reagent for HIV diagnosis.

Supporting Evidence

  • The recombinant p24 protein was highly expressed in soluble form after induction in E. coli.
  • SDS-PAGE analysis showed that the His-tagged recombinant p24 protein was successfully purified.
  • Indirect ELISA demonstrated that the recombinant p24 protein specifically reacted with HIV-infected human serum samples.
  • The immunogenicity of the p24 protein was confirmed by the production of specific antibodies in immunized mice.

Takeaway

Scientists made a special protein from HIV that can help doctors find out if someone is infected with the virus. They tested it on mice and it worked well.

Methodology

The p24 protein was expressed in E. coli, purified using nickel affinity chromatography, and tested for immunogenicity in mice.

Participant Demographics

The study included 90 human serum samples, with 40 HIV-1 positive and 50 HIV-1 negative samples.

Statistical Information

P-Value

p<0.001

Statistical Significance

p<0.001

Digital Object Identifier (DOI)

10.1186/1743-422X-8-316

Want to read the original?

Access the complete publication on the publisher's website

View Original Publication