DOI: 10.1002/1873-3468.14807 ISSN: 0014-5793

The lipid‐binding D4 domain of perfringolysin O facilitates the active loading of exogenous cargo into extracellular vesicles

Abayomi Emmanuel Opadele, Soichiro Nishioka, Ping‐Hsiu Wu, Quynh‐Thu Le, Hiroki Shirato, Jin‐Min Nam, Yasuhito Onodera
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Biochemistry
  • Structural Biology
  • Biophysics

Whereas extracellular vesicles (EVs) have been engineered for cargo loading, innovative strategies for it can still be developed. Here, we describe domain 4 (D4), a cholesterol‐binding domain derived from perfringolysin O, as a viable candidate for EV cargo loading. D4 and its mutants localized to the plasma membrane and the membranes of different vesicular structures in the cytoplasm, and facilitate the transport of proteins of interest (POIs) into EVs. D4‐EVs were internalized by recipient cells analogous to EVs engineered with CD9. Intracellular cargo discharge from D4‐EVs was successfully detected with the assistance of vesicular stomatitis virus glycoprotein. This study presents a novel strategy for recruiting POIs into EVs via a lipid‐binding domain that ensures content release in recipient cells.

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