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Ex Vivo Infection of Murine Epidermis with Herpes Simplex Virus Type 1
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Published on: August 24, 2015

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Parallel Evolution of Chemokine Binding by Structurally Related Herpesvirus Decoy Receptors

Olga Y Lubman1, Daved H Fremont2

  • 1Department of Pathology and Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.

Structure (London, England : 1993)
|December 17, 2015
PubMed

Insights

Rodent herpesvirus R17 protein inhibits host immune responses by binding CC and C chemokines. Structural analysis reveals its unique binding mechanism, distinct from similar viral proteins, highlighting independent evolution of immune evasion strategies.

Area of Science:

  • Virology and Immunology
  • Structural Biology
  • Molecular Mechanisms of Pathogenesis

Background:

  • Pathogens frequently target host chemokine signaling networks to evade immune surveillance and defense.
  • Chemokines are crucial for orchestrating immune cell trafficking and inflammatory responses.

Purpose of the Study:

  • To perform structural and mutational analysis of the R17 protein from rodent herpesvirus Peru.
  • To elucidate the mechanism by which R17 inhibits chemokine signaling and its evolutionary relationship with other viral chemokine decoys.

Main Methods:

  • X-ray crystallography for structural determination of R17.
  • Mutational analysis to identify key residues involved in chemokine binding and complex stability.
  • Biochemical assays to assess binding affinities and kinetics.

Main Results:

  • R17, a potent chemokine inhibitor, binds CC and C chemokines with high affinity.
  • Structural analysis revealed R17 possesses a unique architecture with distinct binding sites for chemokines (e.g., CCL3) and glycosaminoglycans.
  • Chemokine engagement primarily involves N-loop determinants, with the 40s loop contributing to stable complex formation; R17 shares structural similarity but not functional conservation with MHV-68 M3.

Conclusions:

  • R17 effectively neutralizes chemokine activity through a specific structural mechanism, contributing to viral immune evasion.
  • The independent evolution of R17 and M3 suggests diverse strategies employed by viruses to manipulate host immunity.
  • Understanding R17's structure-function relationship provides insights into viral pathogenesis and potential therapeutic targets.

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