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Protein Complex Assembly02:41

Protein Complex Assembly

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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Related Experiment Video

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Structure of HIV-1 Capsid Assemblies by Cryo-electron Microscopy and Iterative Helical Real-space Reconstruction
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Surface loop dynamics in adeno-associated virus capsid assembly.

Nina DiPrimio1, Aravind Asokan, Lakshmanan Govindasamy

  • 1Gene Therapy Center, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599-7352, USA.

Journal of Virology
|March 28, 2008
PubMed
Summary
This summary is machine-generated.

The adeno-associated virus (AAV) HI loop is crucial for capsid assembly and genome packaging. Mutations reveal its importance in viral infectivity and nuclear entry.

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Area of Science:

  • Virology
  • Structural Biology
  • Molecular Biology

Background:

  • The adeno-associated virus (AAV) capsid surface features a prominent HI loop domain.
  • This HI loop varies significantly in amino acid sequence across AAV serotypes, despite conserved residues at the fivefold pore.

Purpose of the Study:

  • To understand the role of the AAV HI loop in capsid assembly, genome packaging, and viral infectivity.
  • To investigate the impact of ablating HI loop interactions with the underlying EF loop.

Main Methods:

  • Generated deletion, insertion, and substitution mutants of the AAV HI loop.
  • Introduced heterologous HI loops from various AAV serotypes and synthetic peptides.
  • Analyzed particle assembly, genome packaging, infectivity, nuclear entry, and VP1 subunit incorporation using confocal microscopy and Western blotting.
  • Performed molecular modeling studies on key mutants.

Main Results:

  • Ablation of the HI loop prevented particle assembly.
  • A substitution mutant (10 glycine residues) assembled particles but failed to package genomes.
  • Mutants with heterologous HI loops showed varied effects on titer and infectivity, with AAV5 HI loop causing assembly defects.
  • A conserved phenylalanine (F661) was critical for infectivity; its mutation (F661G) impaired nuclear entry and VP1 subunit incorporation.
  • Molecular modeling suggested F661 disruption affects interactions with the EF loop, impacting VP1 incorporation at the fivefold axis.

Conclusions:

  • The AAV HI loop, despite sequence variability, is essential for capsid assembly, genome packaging, and VP1 subunit incorporation.
  • The HI loop plays a critical role in viral infectivity, potentially by influencing VP1 phospholipase activity and nuclear entry.
  • The conserved phenylalanine at position 661 is vital for efficient viral infection.