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Flexible Connectors between Capsomer Subunits that Regulate Capsid Assembly.

Mary L Hasek1, Joshua B Maurer1, Roger W Hendrix1

  • 1Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, United States.

Journal of Molecular Biology
|July 15, 2017
PubMed
Summary
This summary is machine-generated.

New ionic interactions within viral protein capsomers, specifically the E153-R210 salt bridge, are crucial for correct icosahedral capsid assembly. Disrupting these links leads to non-functional viral structures like tubes or sheets.

Keywords:
bacteriophage assemblycapsid assemblyprotein structuresalt bridgevirus capsids

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Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Viruses assemble icosahedral capsids using hexameric and pentameric protein subunits (capsomers).
  • Assembly of specific T=7 capsids, like in bacteriophage HK97, relies on precise capsomer positioning and inter-capsomer ionic contacts.
  • Previous studies highlighted the importance of inter-capsomer contacts for capsid formation.

Purpose of the Study:

  • To identify and characterize novel intra-capsomer ionic interactions regulating viral capsid assembly.
  • To elucidate the role of the E-loop and its associated salt bridges in controlling capsomer shape and positioning.
  • To understand how these interactions prevent aberrant assembly pathways.

Main Methods:

  • Site-directed mutagenesis to disrupt specific salt bridges (E153-R210).
  • Analysis of viral assembly using electron microscopy and X-ray crystallography.
  • Phenotypic analysis of mutant viruses to assess assembly defects.
  • Computational modeling to support the proposed assembly mechanism.

Main Results:

  • Identified conserved intra-capsomer salt bridges formed by Glutamate E153 (on the E-loop) and Arginine R210.
  • Mutations disrupting the E153-R210 links resulted in non-viable viruses, forming tubes or sheets instead of capsids.
  • X-ray structures revealed the flexibility of E153-R210 links, which are maintained during capsid maturation.
  • These links were shown to regulate capsomer shape changes essential for correct penton placement and capsid size control.

Conclusions:

  • The E153-R210 salt bridges are critical for regulating viral capsid assembly by controlling capsomer shape.
  • These intra-capsomer interactions prevent premature maturation and aberrant assembly into non-functional structures.
  • The findings provide a new model for viral assembly, emphasizing the role of flexible ionic links in mediating programmed shape changes.
  • The E-loop and its associated interactions may represent a conserved mechanism in other viral systems.