High-Level Expression, Single-Step Immunoaffinity Purification and Characterization of Human Tetraspanin Membrane Protein CD81
2008

High-Level Expression and Purification of Human CD81 Protein

Sample size: 32 publication Evidence: moderate

Author Information

Author(s): Takayama Hidehito, Chelikani Prashen, Reeves Philip J., Zhang Shuguang, Khorana H. Gobind

Primary Institution: Massachusetts Institute of Technology

Hypothesis

Can a tetracycline-inducible system be used for high-level expression and purification of the human CD81 protein?

Conclusion

The study successfully demonstrated a method for high-level expression and purification of the CD81 membrane protein, which could aid in structural analyses.

Supporting Evidence

  • The CD81 receptor was purified to >95% purity using a single-step immunoaffinity method.
  • The affinity of the purified CD81 receptor for HCV-E2 protein was determined to be 3.8±1.2 nM.
  • Confocal microscopy confirmed that the CD81 receptor was correctly localized on the plasma membrane.

Takeaway

The researchers found a way to make a lot of a special protein called CD81, which is important for studying diseases like Hepatitis C.

Methodology

The study used a tetracycline-inducible stable mammalian cell line for high-level expression and a single-step rho-1D4-affinity purification method.

Limitations

The study does not address potential post-translational modifications that may affect the protein's function.

Digital Object Identifier (DOI)

10.1371/journal.pone.0002314

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