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Assemblins as maturational proteases in herpesviruses.

Martin Zühlsdorf1, Winfried Hinrichs1

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Herpesvirus assemblin, a unique protease, is crucial for viral capsid maturation. Inhibitors targeting its dimerization offer a promising strategy for developing new anti-herpesvirus drugs.

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Area of Science:

  • Structural biology
  • Virology
  • Biochemistry

Background:

  • Herpesvirus capsid assembly involves a protein scaffold forming procapsids.
  • Maturation involves protease-induced structural changes, leading to icosahedral capsids for DNA packaging.
  • Herpesvirus maturational protease, assemblin, regulates these processes.

Purpose of the Study:

  • To summarize key information on assemblins, a unique class of proteases.
  • To highlight the structural basis for assemblin activation and inhibition.
  • To underscore the therapeutic potential of targeting assemblin for anti-herpesvirus drug development.

Main Methods:

  • Structural elucidation of dimeric and monomeric assemblin forms using techniques like X-ray crystallography.
  • Biochemical studies to understand protease activity regulation.
  • Identification and structural characterization of dimerization inhibitors.

Main Results:

  • The unique serine-protease fold of assemblins with a catalytic triad (serine, two histidines) has been elucidated.
  • Dimeric structures reveal the mechanism of activation.
  • Monomeric structures and monomer-like structures provide insights into inactive states.
  • Inhibitors targeting the dimerization interface have been identified.

Conclusions:

  • Assemblin structure and function are well-characterized across herpesvirus subfamilies.
  • The structural insights provide a proof-of-principle for developing novel anti-herpesvirus therapeutics.
  • Targeting assemblin dimerization represents a viable strategy for antiviral drug discovery.