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Engineering a Self-Assembled Protein Cage for Targeted Dual Functionalization.

Xiao Ma1,2, Lun Yi1,3, Jiani Li1

  • 1State Key Laboratory of Fine Chemicals, Frontiers Science Centre for Smart Materials Oriented Chemical Engineering, School of Bioengineering, Dalian University of Technology, Dalian 116024, China.

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Summary
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Engineered protein cages can now precisely recruit two different proteins using novel chemistries, reducing variability in synthetic biology and medical applications.

Keywords:
orthogonal bioconjugationprotein scaffoldself-assembled protein cagesynthetic metabolon

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Area of Science:

  • Biotechnology
  • Synthetic Biology
  • Protein Engineering

Background:

  • Self-assembled protein cages are versatile scaffolds for organizing proteins of interest (POIs).
  • Precise attachment of multiple POIs to a single cage remains a challenge, leading to assembly variability.
  • Existing methods lack the specificity required for complex, multi-POI functionalization.

Purpose of the Study:

  • To engineer a novel protein cage, DTMi3ST, capable of independently recruiting two distinct POIs.
  • To demonstrate the controlled dual functionalization of protein cages using orthogonal SpyCatcher/SpyTag and DogCatcher/DogTag chemistries.
  • To validate the platform's utility in both in vitro and intracellular environments, and for constructing functional biological assemblies.

Main Methods:

  • Engineering of the DTMi3ST protein cage with dual recruitment sites.
  • Utilizing SpyCatcher (SC)/SpyTag (ST) and DogCatcher (DC)/DogTag (DT) ligation chemistries for POI attachment.
  • In vitro and live-cell experiments using fluorescent proteins as model POIs.
  • Construction of membrane-bound enzyme assemblies in *Escherichia coli*.

Main Results:

  • Demonstrated controlled, independent recruitment of two different POIs to the DTMi3ST protein cage.
  • Successful dual functionalization of protein cages both in vitro and within living cells.
  • Engineered membrane-bound enzyme assemblies in *E. coli* using the functionalized cages.
  • Achieved a 69.6% enhancement in substrate utilization across the bacterial membrane.

Conclusions:

  • The engineered DTMi3ST protein cage platform enables precise dual functionalization, reducing assembly variability.
  • This versatile nanotool facilitates the construction of complex, functional protein assemblies for biological and biomedical applications.
  • The platform shows significant potential for advancing synthetic biology and medical science through controlled protein organization.