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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Human immunodeficiency virus 1 (HIV-1) uses nuclear pore complexes (NPCs) to enter host cell nuclei. Researchers developed NPC mimics to reveal how HIV-1 capsids dock, insert, and penetrate NPCs during nuclear import.

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Area of Science:

  • Virology
  • Cell Biology
  • Biophysics

Background:

  • Nuclear pore complex (NPC) passage is essential for human immunodeficiency virus 1 (HIV-1) infection.
  • The precise mechanism of viral nuclear entry via the NPC is not fully understood due to its complexity.

Purpose of the Study:

  • To elucidate the mechanism of HIV-1 nuclear import through the NPC.
  • To develop a novel system for modeling viral entry into the host cell nucleus.

Main Methods:

  • Construction of DNA-origami-based NPC mimics with programmable nucleoporin arrangements.
  • Utilizing these mimics to study the interactions between HIV-1 capsids and nucleoporins.

Main Results:

  • Identified Nup358 as crucial for initial capsid docking to the NPC's cytoplasm-facing side.
  • Nup153 preferentially binds to capsid curvature, facilitating tip-leading insertion.
  • An affinity gradient created by differential Nup358 and Nup153 binding drives capsid penetration.
  • Nup62 acts as a barrier within the NPC central channel.

Conclusions:

  • The study provides mechanistic insights into HIV-1 nuclear import.
  • Developed a versatile toolset for studying viral nuclear entry mechanisms.