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Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins

Author

Listed:
  • Alexander Harjung

    (University of California)

  • Alessandro Fracassi

    (University of California)

  • Neal K. Devaraj

    (University of California)

Abstract

The development of artificial cells has led to fundamental insights into the functional processes of living cells while simultaneously paving the way for transformative applications in biotechnology and medicine. A common method of generating artificial cells is to encapsulate protein expression systems within lipid vesicles. However, to communicate with the external environment, protein translocation across lipid membranes must take place. In living cells, protein transport across membranes is achieved with the aid of complex translocase systems which are difficult to reconstitute into artificial cells. Thus, there is need for simple mechanisms by which proteins can be encoded and expressed inside synthetic compartments yet still be externally displayed. Here we present a genetically encodable membrane functionalization system based on mutants of pore-forming proteins. We modify the membrane translocating loop of α-hemolysin to translocate functional peptides up to 52 amino acids across lipid membranes. Full membrane translocation occurs in the absence of any translocase machinery and the translocated peptides are recognized by specific peptide-binding ligands on the opposing membrane side. Engineered hemolysins can be used for genetically programming artificial cells to display interacting peptide pairs, enabling their assembly into artificial tissue-like structures.

Suggested Citation

  • Alexander Harjung & Alessandro Fracassi & Neal K. Devaraj, 2024. "Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
  • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53783-4
    DOI: 10.1038/s41467-024-53783-4
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    References listed on IDEAS

    as
    1. Shiksha Mantri & K. Tanuj Sapra & Stephen Cheley & Thomas H. Sharp & Hagan Bayley, 2013. "An engineered dimeric protein pore that spans adjacent lipid bilayers," Nature Communications, Nature, vol. 4(1), pages 1-10, June.
    2. Siew Siew Pang & Charles Bayly-Jones & Mazdak Radjainia & Bradley A. Spicer & Ruby H. P. Law & Adrian W. Hodel & Edward S. Parsons & Susan M. Ekkel & Paul J. Conroy & Georg Ramm & Hariprasad Venugopal, 2019. "The cryo-EM structure of the acid activatable pore-forming immune effector Macrophage-expressed gene 1," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
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