ArticleJournal of virology1998
Herpes simplex virus 1 regulatory protein ICP22 interacts with a new cell cycle-regulated factor and accumulates in a cell cycle-dependent fashion in infected cells.
Article in Journal of virology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 53 citations in OpenAlex.
- The Herpes Simplex Virus 1 Immediate Early Protein ICP22 Is a Functional Mimic of a Cellular J Protein.Journal of virology · 2020Article
- Roles of p53 in herpes simplex virus 1 replication.Journal of virology · 2013Article
- Herpes simplex virus 1 ICP22 inhibits the transcription of viral gene promoters by binding to and blocking the recruitment of P-TEFb.PloS one · 2012Article
- Characterization of the interaction between human respiratory syncytial virus and the cell cycle in continuous cell culture and primary human airway epithelial cells.Journal of virology · 2011Article
- Sequence variation in the herpes simplex virus U(S)1 ocular virulence determinant.Investigative ophthalmology & visual science · 2011Article
- The herpes simplex virus type 1 infected cell protein 22.Virologica Sinica · 2010Review
- MCRS2 represses the transactivation activities of Nrf1.BMC cell biology · 2009Article
- Repressor element-1 silencing transcription factor/neuronal restrictive silencer factor (REST/NRSF) can regulate HSV-1 immediate-early transcription via histone modification.Virology journal · 2007Article
- Herpes simplex virus immediate-early protein ICP22 triggers loss of serine 2-phosphorylated RNA polymerase II.Journal of virology · 2007Article
- ICP22 is required for wild-type composition and infectivity of herpes simplex virus type 1 virions.Journal of virology · 2006Article
- p78/MCRS1 forms a complex with centrosomal protein Nde1 and is essential for cell viability.Oncogene · 2006Article
- The products of the herpes simplex virus type 1 immediate-early US1/US1.5 genes downregulate levels of S-phase-specific cyclins and facilitate virus replication in S-phase Vero cells.Journal of virology · 2006Article
- Cellular transformation by the MSP58 oncogene is inhibited by its physical interaction with the PTEN tumor suppressor.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Immediate-early expression of the herpes simplex virus type 1 ICP27 transcript is not critical for efficient replication in vitro or in vivo.Journal of virology · 2004Article
- Article
- The EICP22 protein of equine herpesvirus 1 physically interacts with the immediate-early protein and with itself to form dimers and higher-order complexes.Journal of virology · 2000Article
- The disappearance of cyclins A and B and the increase in activity of the G(2)/M-phase cellular kinase cdc2 in herpes simplex virus 1-infected cells require expression of the alpha22/U(S)1.5 and U(L)13 viral genes.Journal of virology · 2000Article
- Early expression of herpes simplex virus (HSV) proteins and reactivation of latent infection.Folia microbiologica · 2000Review
- HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Neoplasia (New York, N.Y.) · 1999Review
- Perturbation of cell cycle progression and cellular gene expression as a function of herpes simplex virus ICP0.Journal of virology · 1999Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The herpes simplex virus 1 infected cell protein 22 (ICP22), the product of the alpha22 gene, is a nucleotidylylated and phosphorylated nuclear protein with properties of a transcriptional factor required for the expression of a subset of viral genes. Here, we report the following. (i) ICP22 interacts with a previously unknown cellular factor designated p78 in the yeast two-hybrid system. The p78 cDNA encodes a polypeptide with a distribution of leucines reminiscent of a leucine zipper. (ii) In uninfected and infected cells, antibody to p78 reacts with two major bands with an apparent Mr of 78,000 and two minor bands with apparent Mrs of 62, 000 and 55,000. (ii) p78 also interacts with ICP22 in vitro. (iii) In uninfected cells, p78 was dispersed largely in the nucleoplasm in HeLa cells and in the nucleoplasm and cytoplasm in HEp-2 cells. After infection, p78 formed large dense bodies which did not colocalize with the viral regulatory protein ICP0. (iv) Accumulation of p78 was cell cycle dependent, being highest very early in S phase. (v) The accumulation of ICP22 in synchronized cells was highest in early S phase, in contrast to the accumulation of another protein, ICP27, which was relatively independent of the cell cycle. (vi) In the course of the cell cycle, ICP22 was transiently modified in an aberrant fashion, and this modification coincided with expression of p78. The results suggest that ICP22 interacts with and may be stabilized by cell cycle-dependent proteins.
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