Substrate specificity of the herpes simplex virus type 2 UL13 protein kinase

Gina L Cano-Monreal1, John E Tavis, Lynda A Morrison

  • 1Department of Molecular Microbiology and Immunology, Saint Louis University School of Medicine, 1100 South Grand Blvd., St. Louis, MO 63104, USA. canogl@slu.edu

Virology
|January 22, 2008
PubMed

Insights

Herpes simplex virus type 2 UL13 protein kinase autophosphorylates and recognizes a simple serine-proline motif. Its substrate specificity is not mimicked by ERK or Cdc2, suggesting other factors influence recognition.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • The UL13 protein kinase is a conserved protein among herpesviruses.
  • The specific substrates and recognition motifs for HSV-2 UL13 are not well understood.

Purpose of the Study:

  • To investigate the substrate specificity and recognition mechanisms of HSV-2 UL13.
  • To determine if HSV-2 UL13 mimics known kinase motifs like ERK or Cdc2.

Main Methods:

  • Characterization of HSV-2 UL13 as a phosphoprotein and its autophosphorylation activity.
  • Peptide phosphorylation assays using wild-type and mutated peptides to identify recognition motifs.
  • Comparative analysis of HSV-2 UL13 phosphorylation against ERK and Cdc2 consensus motifs.

Main Results:

  • HSV-2 UL13 is a phosphoprotein that autophosphorylates.
  • Serines in ERK and Cdc2 motifs are important for autophosphorylation but not exogenous substrate phosphorylation.
  • HSV-2 UL13 phosphorylates a minimal serine-proline motif, distinct from ERK and Cdc2 recognition.
  • Mutation of prolines near the phosphoacceptor site reduced phosphorylation by HSV-2 UL13.

Conclusions:

  • HSV-2 UL13 does not mimic ERK or Cdc2 substrate recognition patterns.
  • The minimal recognition motif for HSV-2 UL13 is serine-proline.
  • Substrate specificity is likely influenced by sequences or structural elements outside the minimal motif.

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