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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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Updated: Aug 29, 2025

Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods
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Structure-function analysis of enterovirus protease 2A in complex with its essential host factor SETD3.

Christine E Peters1, Ursula Schulze-Gahmen2,3,4, Manon Eckhardt3,4,5,6

  • 1Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA, USA.

Nature Communications
|September 8, 2022
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Summary
This summary is machine-generated.

Researchers identified a key interaction between host factor SETD3 and enterovirus protease 2A. Blocking this interaction completely protected cells from enteroviral infection, offering a new therapeutic strategy.

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Area of Science:

  • Virology
  • Structural Biology
  • Host-Pathogen Interactions

Background:

  • Enteroviruses cause significant human diseases, yet lack approved antiviral treatments.
  • Host-directed therapies offer a promising alternative for treating enteroviral infections.
  • SETD3 (actin histidine methyltransferase) was previously identified as a host factor interacting with enterovirus protease 2A.

Purpose of the Study:

  • To elucidate the molecular mechanism of the SETD3-enterovirus 2A interaction.
  • To provide a structural basis for developing host-directed therapeutics against enteroviruses.

Main Methods:

  • Determined the cryo-electron microscopy (cryo-EM) structure of SETD3 bound to coxsackievirus B3 2A at 3.5 Å resolution.
  • Performed structure-function analysis by mutating key residues within the SET domain of SETD3.
  • Assessed the impact of mutations on SETD3-2A binding and viral protection.

Main Results:

  • Revealed the cryo-EM structure of SETD3 interacting with coxsackievirus B3 2A at two distinct interfaces, including the SET domain's substrate-binding surface.
  • Mutations in the SET domain significantly reduced SETD3 binding to viral 2A.
  • These mutations conferred complete protection against enteroviral infection.

Conclusions:

  • The study provides critical molecular insights into the SETD3-2A interaction.
  • The findings establish a structural framework for designing novel host-directed therapeutics targeting enteroviral diseases.
  • Targeting the SETD3-2A interface represents a viable strategy for developing antiviral therapies.