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

Virology
Gina L Cano-MonrealLynda A Morrison

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.

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Citations

Nov 19, 2010·Journal of Virology·Thary JacobHerman W Favoreel
Sep 24, 2011·Nucleus·Lynda A Morrison, Gregory S DeLassus
Jul 31, 2009·Virology·Gina L Cano-MonrealLynda A Morrison
May 4, 2012·The Journal of General Virology·Rachel B GillMark N Prichard
Sep 17, 2020·Veterinary Research·Zongyi BoJianjun Dai

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