Literature DB >> 10364384

Identification of phosphorylation sites within the herpes simplex virus tegument protein VP22.

G Elliott1, D O'Reilly, P O'Hare.   

Abstract

The herpes simplex virus protein VP22 is a major phosphoprotein of infected cells. In this study, we identify two serine phosphorylation sites within VP22 and show that the N-terminal site is a substrate for casein kinase II, while the extreme C-terminal site is a substrate for another, as yet unidentified, cellular kinase. Furthermore, we show that a mutant of VP22 which has both sites altered is unable to incorporate phosphate in vivo, confirming that there are no other phosphorylation sites within VP22.

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Year:  1999        PMID: 10364384      PMCID: PMC112693     

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  10 in total

1.  The herpes simplex virus type 1 tegument protein VP22 is encoded by gene UL49.

Authors:  G D Elliott; D M Meredith
Journal:  J Gen Virol       Date:  1992-03       Impact factor: 3.891

2.  Overexpression of the herpes simplex virus type 1 tegument protein VP22 increases its incorporation into virus particles.

Authors:  J Leslie; F J Rixon; J McLauchlan
Journal:  Virology       Date:  1996-06-01       Impact factor: 3.616

3.  Intercellular trafficking and protein delivery by a herpesvirus structural protein.

Authors:  G Elliott; P O'Hare
Journal:  Cell       Date:  1997-01-24       Impact factor: 41.582

4.  Phosphorylation of the herpes simplex virus type 1 tegument protein VP22.

Authors:  G Elliott; D O'Reilly; P O'Hare
Journal:  Virology       Date:  1996-12-01       Impact factor: 3.616

5.  Proteins specified by herpes simplex virus. Staining and radiolabeling properties of B capsid and virion proteins in polyacrylamide gels.

Authors:  W Gibson; B Roizman
Journal:  J Virol       Date:  1974-01       Impact factor: 5.103

6.  Proteins specified by herpes simplex virus. V. Purification and structural proteins of the herpesvirion.

Authors:  P G Spear; B Roizman
Journal:  J Virol       Date:  1972-01       Impact factor: 5.103

7.  VP16 interacts via its activation domain with VP22, a tegument protein of herpes simplex virus, and is relocated to a novel macromolecular assembly in coexpressing cells.

Authors:  G Elliott; G Mouzakitis; P O'Hare
Journal:  J Virol       Date:  1995-12       Impact factor: 5.103

8.  Virus-specific basic phosphoproteins associated with herpes simplex virus type a (HSV-1) particles and the chromatin of HSV-1-infected cells.

Authors:  K W Knopf; H C Kaerner
Journal:  J Gen Virol       Date:  1980-02       Impact factor: 3.891

9.  Herpes simplex virus type 1 tegument protein VP22 induces the stabilization and hyperacetylation of microtubules.

Authors:  G Elliott; P O'Hare
Journal:  J Virol       Date:  1998-08       Impact factor: 5.103

10.  Phosphorylation of structural components promotes dissociation of the herpes simplex virus type 1 tegument.

Authors:  E E Morrison; Y F Wang; D M Meredith
Journal:  J Virol       Date:  1998-09       Impact factor: 5.103

  10 in total
  20 in total

1.  Cytoplasm-to-nucleus translocation of a herpesvirus tegument protein during cell division.

Authors:  G Elliott; P O'Hare
Journal:  J Virol       Date:  2000-03       Impact factor: 5.103

2.  Herpes simplex virus tegument protein VP22 contains overlapping domains for cytoplasmic localization, microtubule interaction, and chromatin binding.

Authors:  Ana Martin; Peter O'Hare; John McLauchlan; Gillian Elliott
Journal:  J Virol       Date:  2002-05       Impact factor: 5.103

3.  Assembly of infectious Herpes simplex virus type 1 virions in the absence of full-length VP22.

Authors:  L E Pomeranz; J A Blaho
Journal:  J Virol       Date:  2000-11       Impact factor: 5.103

4.  Distinctions between bovine herpesvirus 1 and herpes simplex virus type 1 VP22 tegument protein subcellular associations.

Authors:  J S Harms; X Ren; S C Oliveira; G A Splitter
Journal:  J Virol       Date:  2000-04       Impact factor: 5.103

5.  Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase.

Authors:  Maria Teresa Sciortino; Brunella Taddeo; Maria Giuffrè-Cuculletto; Maria Antonietta Medici; Antonio Mastino; Bernard Roizman
Journal:  J Virol       Date:  2007-08-01       Impact factor: 5.103

6.  Characterization of VP22 in herpes simplex virus-infected cells.

Authors:  G Mouzakitis; John McLauchlan; Cristina Barreca; Lisa Kueltzo; P O'Hare
Journal:  J Virol       Date:  2005-10       Impact factor: 5.103

7.  Elucidation of the block to herpes simplex virus egress in the absence of tegument protein UL16 reveals a novel interaction with VP22.

Authors:  Jason L Starkey; Jun Han; Pooja Chadha; Jacob A Marsh; John W Wills
Journal:  J Virol       Date:  2013-10-16       Impact factor: 5.103

8.  The pseudorabies virus VP22 homologue (UL49) is dispensable for virus growth in vitro and has no effect on virulence and neuronal spread in rodents.

Authors:  T del Rio; H C Werner; L W Enquist
Journal:  J Virol       Date:  2002-01       Impact factor: 5.103

9.  Temporal regulation of herpes simplex virus type 2 VP22 expression and phosphorylation.

Authors:  B J Geiss; J E Tavis; L M Metzger; D A Leib; L A Morrison
Journal:  J Virol       Date:  2001-11       Impact factor: 5.103

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

Authors:  Gina L Cano-Monreal; John E Tavis; Lynda A Morrison
Journal:  Virology       Date:  2008-01-22       Impact factor: 3.616

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