Hiring in life sciences? Share your open positions with our professional community. Read more Close

Advertisement

Cargo-directed assembly of nonviral nucleocapsid with controlled size

Created on 08 Nov 2025

Authors

Tajima, K., Sakai, Y., Terasaka, N.

Abstract

Precise packaging of diverse cargo within self-assembling protein cages of defined size and shape is essential for many biotechnological applications, yet cellular expression offers limited control over loading. Here, we developed a system for in vitro cargo-directed reconstitution of a split, laboratory evolved nonviral nucleocapsid (spNC-4). Independently expressed and purified spNC-4 capsid protein subunits were mixed and assembled with cargo molecules in a cooperative manner. As an authentic cargo, mRNA is packaged into a 30 nm-spheric nucleocapsid in vitro, closely matching to spNC-4 expressed in cells. In this system, a diverse range of cargo molecules, including cognate nucleocapsid mRNA, noncognate RNA, RNA complexed with positively supercharged fluorescent protein, and linear double-stranded DNA are encapsulated within the 30 nm-spheric nucleocapsids in vitro. Moreover, the packaging of 30 nm-spherical or rod-shaped DNA origamis as templates induce morphological alterations of the nucleocapsids, resulting in the formation of enlarged 60 nm-spherical structure or rod-shaped structure, respectively. This split-protein, cargo-dependent system provides versatile and programmable control over both composition and architecture of nonviral protein cages, creating a general platform for enzyme nanoreactors, targeted delivery, and vaccine development.

Preprint server: bioRxiv
The authors list and abstract were imported from bioRxiv on 08 Nov 2025.

Advertisement

Stats

  • Community rating n/a 0 votes
  • Your rating

1-terrible, 9-excellent. How would you rate this preprint? Sign in in to submit your rating.

  • Recommendations n/a n/a positive of 0 vote(s)
  • Views 32
  • Comments 0

Recommended by

  • No recommendations yet.

Post a comment

You need to be signed in to post comments. You can sign in here.

Comments

There are no comments yet.

Advertisement