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Related Concept Videos

Viral Structure00:56

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Viruses are extraordinarily diverse in shape and size, but they all have several structural features in common. All viruses have a core that contains a DNA- or RNA-based genome. The core is surrounded by a protective coat of proteins called the capsid. The capsid is composed of subunits called capsomeres. The capsid and genome-containing core are together known as the nucleocapsid.
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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Retroviruses have a single-stranded RNA genome that undergoes a special form of replication. Once the retrovirus has entered the host cell, an enzyme called reverse transcriptase synthesizes double-stranded DNA from the retroviral RNA genome. This DNA copy of the genome is then integrated into the host’s genome inside the nucleus via an enzyme called integrase. Consequently, the retroviral genome is transcribed into RNA whenever the host’s genome is transcribed, allowing the...
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Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Stimulus-responsive assembly of nonviral nucleocapsids.

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Researchers developed a method to control protein shell assembly around RNA. By blocking and then triggering protein cage formation with enzymes, they created ordered nucleocapsids for potential use in studying viral and nonviral assemblies.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Virology

Background:

  • Controlled assembly of protein shells around genetic material is crucial for viral replication.
  • Existing methods for in vitro nucleocapsid formation have limitations in cargo encapsulation and assembly control.

Purpose of the Study:

  • To develop a strategy for regulating the co-assembly of nonviral proteins and nucleic acids into ordered nucleocapsids in vitro.
  • To enable controlled, RNA-templated formation of engineered protein cages.

Main Methods:

  • Engineered an NC-4 protein cage by fusing maltose binding protein to its subunits to block spontaneous assembly.
  • Utilized selective proteolysis to remove the steric block and initiate RNA-templated capsid formation.
  • Employed transmission and cryo-electron microscopy to analyze the structure of the assembled nucleocapsids.

Main Results:

  • Successfully blocked spontaneous capsid assembly, allowing isolation of soluble protein monomers.
  • Achieved RNA-templated nucleocapsid formation upon enzymatic trigger, producing structures identical to in vivo assemblies.
  • Demonstrated that the method allows for broader RNA encapsulation by the NC-4 cage.

Conclusions:

  • Enzymatically triggered protein cage formation offers a novel method for controlled nucleocapsid assembly.
  • This approach provides new opportunities to study the co-assembly of viral/nonviral capsids and their genetic cargo.
  • The technique has potential applications in studying diverse viral and nonviral assembly processes.