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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
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Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
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Sortase A-Based Post-translational Modifications on Encapsulin Nanocompartments.

Seyed Hossein Helalat1, Rodrigo Coronel Téllez1, Ehsan Ansari Dezfouli1

  • 1Department of Health Technology, Technical University of Denmark, Ørsteds Plads, DK-2800 Kgs. Lyngby, Denmark.

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Summary

Researchers engineered protein-based encapsulin nanoparticles using a novel enzymatic ligation system. This method allows site-specific protein attachment internally and externally without in vitro steps, advancing biotechnology and nanomedicine applications.

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Area of Science:

  • Biotechnology and Nanomedicine
  • Protein Engineering
  • Enzymatic Ligation

Background:

  • Protein-based encapsulin nanocompartments offer structural integrity and functional versatility.
  • Current methods for modifying encapsulins often require complex in vitro procedures.
  • Site-specific protein conjugation is crucial for developing advanced nanomedical tools.

Purpose of the Study:

  • To develop an efficient in vivo system for site-specific protein attachment to encapsulins.
  • To explore the use of sortase A-mediated ligation for internal and external protein conjugation.
  • To demonstrate the applicability of this system for creating functionalized encapsulin nanoparticles.

Main Methods:

  • Engineered a sortase A-mediated protein ligation system within Escherichia coli.
  • Fused sortase enzyme and protease for post-translational ligation of target proteins (e.g., GFP, anti-CD3 scFv) to encapsulins.
  • Investigated protein attachment to both the exterior surface and interior of encapsulin nanocompartments.

Main Results:

  • Successfully achieved site-specific protein attachment to encapsulins without affecting protein folding or assembly.
  • Demonstrated successful conjugation of proteins to the exterior surface of encapsulin nanoparticles.
  • Showed that internal protein loading can alter nanoparticle size and shape due to cargo overload.

Conclusions:

  • Developed a novel enzymatic ligation method for engineering encapsulin nanoparticles.
  • The system enables efficient in vivo protein conjugation, simplifying nanoparticle functionalization.
  • This approach provides a versatile platform for creating advanced biotechnological and nanomedical tools.