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Engineering Fibroblast Growth Factor-2 (FGF2) Production in Cyanobacteria.

Bharat Kumar Majhi1, Anastasios Melis1

  • 1Department of Plant and Microbial Biology, 111 Koshland Hall, MC-3102, University of California, Berkeley, California 94720-3102, United States.

ACS Synthetic Biology
|October 4, 2025
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Summary
This summary is machine-generated.

Recombinant Fibroblast Growth Factor 2 (FGF2) was stabilized and accumulated in cyanobacteria by fusing it with phycocyanin. This overcomes expression challenges for difficult proteins, enabling bioactivity.

Keywords:
DNA and protein fusion constructsSynechocystis sp. PCC 6803phycocyaninprotein overexpressionrecombinant protein

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Area of Science:

  • Biotechnology
  • Synthetic Biology
  • Protein Engineering

Background:

  • Fibroblast Growth Factor 2 (FGF2) is crucial for cell growth, division, and repair, with applications in biomedicine.
  • FGF2's unique β-barrel structure, composed solely of β-pleated sheets, poses challenges for stable expression and isolation in heterologous systems.
  • Cyanobacteria, like *Synechocystis* sp. PCC 6803, are model organisms for photosynthesis and synthetic biology research.

Purpose of the Study:

  • To develop a method for stable recombinant FGF2 accumulation in *Synechocystis*.
  • To overcome the expression difficulties associated with FGF2's β-sheet-rich structure.
  • To demonstrate the utility of phycocyanin fusion for enhancing the expression of challenging recombinant proteins.

Main Methods:

  • Codon-optimized FGF2 gene was fused with the CpcB β-subunit of phycocyanin.
  • The fusion construct was expressed in *Synechocystis* sp. PCC 6803.
  • Bioactivity of the resulting phycocyanin-FGF2 fusion protein (Phyco*FGF2) was assessed.

Main Results:

  • Stable accumulation of recombinant FGF2 was achieved in *Synechocystis*.
  • The fusion strategy successfully stabilized the FGF2 protein, overcoming structural challenges.
  • The recombinant Phyco*FGF2 fusion protein retained both phycocyanin and FGF2 bioactivity.
  • Stoichiometric accumulation of the fusion protein was observed.

Conclusions:

  • Cyanobacterial systems can successfully express difficult-to-express heterologous proteins when fused to phycocyanin.
  • Phycocyanin fusion enhances the stability and accumulation of recombinant proteins like FGF2.
  • This approach offers a viable strategy for producing functional recombinant proteins in cyanobacteria for biotechnological applications.