Related Experiment Video
Updated: Jul 8, 2026

Purification of Viral DNA for the Identification of Associated Viral and Cellular Proteins
Published on: August 31, 2017
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
Abstract:
The UL13 protein kinase is conserved among many herpesviruses but HSV-2 UL13 specificity is not known. Here, we found that HSV-2 UL13 is a phosphoprotein that autophosphorylates, and that serines within ERK and Cdc2 motifs were important for autophosphorylation but not for UL13 phosphorylation of exogenous substrates. HSV-2 UL13 phosphorylated a peptide also recognized by ERK and Cdc2. However, mutation of substrate residues critical for Cdc2 or Erk phosphorylation did not alter HSV-2 UL13 phosphorylation of the peptide, and HSV-2 UL13 did not phosphorylate standard Cdc2 or Erk peptide substrates. Mutation of prolines surrounding the peptide phosphoacceptor site reduced phosphorylation by HSV-2 UL13, and a peptide containing serine-proline amid alanines and glycines was phosphorylated. Thus, HSV-2 UL13 does not mimic ERK or Cdc2 substrate recognition and its minimal recognition motif can be serine-proline. This motif's simplicity indicates that distal sequence or protein structure contributes to HSV-2 UL13 substrate specificity.
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.
More Related Videos
Related Concept Videos
Herpes
Antiviral Nucleoside Inhibitors
Inhibitors of Viral Protein Synthesis
Genital Herpes

