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Related Experiment Videos

Structure and function of recombinant cobra venom factor.

Michael A Kock1, Brian E Hew, Holger Bammert

  • 1Department of Biochemistry and Molecular Biology, University of Hamburg, 20146 Hamburg, Germany.

The Journal of Biological Chemistry
|May 8, 2004
PubMed
Summary

Recombinant expression of cobra venom factor (CVF) yields active protein, ensuring a vital research reagent for complement depletion. This breakthrough overcomes challenges with sourcing natural CVF from endangered species.

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Area of Science:

  • Immunology and Biochemistry
  • Recombinant protein expression
  • Complement system research

Background:

  • Cobra venom factor (CVF) is a complement-activating protein, functionally analogous to complement component C3b.
  • CVF acts as a C3/C5 convertase, cleaving complement components C3 and C5.
  • Natural CVF is sourced from cobra venom, posing supply challenges due to endangered species status.

Purpose of the Study:

  • To report the recombinant expression of pro-CVF in insect cell systems.
  • To characterize the functional activity of recombinantly expressed pro-CVF.
  • To establish a sustainable source of active CVF for research and therapeutic development.

Main Methods:

  • Recombinant expression of pro-CVF using baculovirus-infected Sf9 cells and stably transfected S2 Drosophila cells.

Related Experiment Videos

  • Analysis of pro-CVF processing into different molecular forms.
  • Functional assays to assess factor B activation and complement depletion activity of pro-CVF.

    • Main Results:

    • Pro-CVF was synthesized and processed into multiple forms in insect cells, resembling C3 and C3b.
    • All recombinant pro-CVF forms exhibited functional activity identical to mature, natural CVF.
    • Recombinant pro-CVF formed an active C3/C5 convertase (pro-CVF,Bb) with C3 and C5 cleaving capabilities.

    Conclusions:

    • Recombinant expression provides a reliable and sustainable source of active CVF, crucial for complement research.
    • This method addresses the scarcity of natural CVF from endangered cobras.
    • Recombinant pro-CVF is valuable for studying CVF structure-function relationships and developing therapeutic complement inhibitors.