The Products of Gene US11 of Herpes Simplex Virus Type 1 Are DNA-binding and Localize to the Nucleoli of Infected Cells

MacLean, Christine A.; Rixon, Frazer J.; Marsden, Howard S.

doi:10.1099/0022-1317-68-7-1921

Cited by 55 publications

(52 citation statements)

References 21 publications

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“…For comparison, the behaviour of two other proteins was also examined: 21K, a true late protein (Johnson et al, 1986) and 65KDBP, an early protein (Schenk & Ludwig, 1988;Goodrich et al, t989) whose synthesis is reduced three-to four-fold in the presence of PAA (Goodrich et al, 1989). The reactivities on Western blots of the rabbit antisera 18826 and 14327 when used to detect expression of 65KDBp and 21K respectively have previously been described (Parris et al, 1988;MacLean et al, 1987). Antiserum 18826 reacts with only a single protein, 65KDBp (Parris et al, 1988), whereas antiserum 14327 reacts with predominantly 21K and proteins of apparent MT 22K, 17-5K, 14K and 11K, which have been shown to be related to 21K (MacLean et al, 1987).…”

Section: Resultsmentioning

confidence: 88%

“…The reactivities on Western blots of the rabbit antisera 18826 and 14327 when used to detect expression of 65KDBp and 21K respectively have previously been described (Parris et al, 1988;MacLean et al, 1987). Antiserum 18826 reacts with only a single protein, 65KDBp (Parris et al, 1988), whereas antiserum 14327 reacts with predominantly 21K and proteins of apparent MT 22K, 17-5K, 14K and 11K, which have been shown to be related to 21K (MacLean et al, 1987). The results of this experiment are shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Animals were bled on day 50. Antiserum 18826, prepared against a synthetic oligopeptide corresponding to amino acids 476 to 487 of the 65K DNA-binding protein encoded by UL42, has previously been described (Parris et al, 1988), as has antiserum 14327, which was prepared against a synthetic oligopeptide corresponding to amino acids 151 to 161 of the predicted US11 gene product (MacLean et al, 1987).…”

Section: G Mclean and Othersmentioning

confidence: 99%

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Identification and Characterization of the Virion Protein Products of Herpes Simplex Virus Type 1 Gene UL47

McLean

Rixon

Langeland

et al. 1990

Journal of General Virology

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Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 99%

Section: G Mclean and Othersmentioning

confidence: 99%

See 1 more Smart Citation

Identification and Characterization of the Virion Protein Products of Herpes Simplex Virus Type 1 Gene UL47

McLean

Rixon

Langeland

et al. 1990

Journal of General Virology

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“…It has been proposed that the herpesvirus saimiri ORF57 protein uses nucleoli to export intronless viral messages (Boyne and Whitehouse, 2006;Williams et al, 2005). The HSV-1 ICP27, ICP0, γ 1 34.5, and U S 11 proteins were reported to possess nucleolar targeting sequences (Cheng et al, 2002;MacLean et al, 1987;Mears et al, 1995;Morency et al, 2005) but the implications of these are unknown. Emerging evidence now argues that nucleoli act as a cellular stress sensor which functions to regulate p53 and cell cycle arrest (Mayer et al, 2005;Rubbi and Milner, 2003).…”

Section: Vp22 Targets Nucleolinmentioning

confidence: 99%

“…The molecular mechanism of HSV-1 tegument and envelope assembly is poorly understood. Most of the major tegument proteins, especially VP22, exhibit a nuclear distribution late in infection (Albright and Jenkins, 1993;Chang and Roizman, 1993;Conley et al, 1981;Cunningham et al, 2000;Daikoku et al, 1998;Daikoku et al, 1997;MacLean et al, 1987;Morrison et al, 1998;Naldinho-Souto et al, 2006;Pomeranz and Blaho, 1999;Taus et al, 1998) and there is general agreement that primary envelopment occurs as the capsid exits the nucleus (Browne et al, 1996;Gershon et al, 1994;Granzow et al, 1997;Stackpole, 1969;Whiteley et al, 1999) {reviewed in (Enquist et al, 1998;Mettenleiter, 2002)}.…”

Section: Introductionmentioning

confidence: 99%

The major tegument structural protein VP22 targets areas of dispersed nucleolin and marginalized chromatin during productive herpes simplex virus 1 infection

et al. 2008

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The HSV major tegument structural protein VP22 resides in multiple subcellular regions during productive infection. During an analysis of the molecular determinants of these localizations, we observed that a transfected fusion of the C-terminal portion of VP22, containing its pat4 nuclear localization signal, with GFP lacked nucleolar sparing compared to GFP alone. Thus, the initial goal was to determine whetherr VP22 associates with nucleoli. Using an optimized indirect immunofluorescence system to visualize nucleolin and viral proteins, we observed that VP22 present in VP22-expressing Vero (V49) cells "surrounded" nucleolin. These two initial findings implied that VP22 might associate directly with nucleoli. We next analyzed HSV infected cells and observed that at late times, anti-nucleolin immune reactivity was dispersed throughout the nuclei while it retained uniform, circular staining in mock-infected cells. Time course infection experiments indicated that nucleolin initiated its transition from uniform to dispersed structures between 2 and 4 hpi. Comparison of Hoechst stained nuclei showed bright anti-nucleolin staining localized to regions of marginalized chromatin. These effects required de novo infected cell protein synthesis. A portion of VP22 detected in nuclei at 4 and 6 hpi localized to these areas of altered nucleolin and marginalized chromatin. VP22 was excluded from viral replication compartments containing the viral regulatory protein ICP22. Finally, altered nucleolin and marginalized chromatin were detected with a VP22-null virus, indicating that VP22 was not responsible for these nuclear architecture alterations. Thus, we conclude that nuclear VP22 targets unique subnuclear structures early (< 6 hpi) during HSV-1 infection.

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Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression

et al. 1995

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The Us11 protein is a true late gene product of herpes simplex virus type 1 (HSV-1), whose exact function is unknown but which exhibits RNA-binding properties and which is phosphorylated on serine residues. In order to determine whether the Us11 protein is phosphorylated by cellular kinase(s) or by virally encoded kinase(s), the Us11 gene has been cloned and transiently expressed in HeLa cells. In addition, HeLa-derived cell lines have been selected for their ability to express Us11 protein constitutively. 32P-Labeling and analysis by two-dimensional electrophoresis of transiently and constitutively expressed Us11 protein demonstrated that, indeed, multiple phosphorylation of the protein occurs in absence of HSV-1 genome expression, indicating that the protein behaves as a natural substrate for cellular kinase(s). In addition, a sequence heterogeneity of the Us11 protein, due to a difference in the number of SPREPR repeats, has been characterized between different strains of HSV-1.

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The Products of Gene US11 of Herpes Simplex Virus Type 1 Are DNA-binding and Localize to the Nucleoli of Infected Cells

Cited by 55 publications

References 21 publications

Identification and Characterization of the Virion Protein Products of Herpes Simplex Virus Type 1 Gene UL47

Identification and Characterization of the Virion Protein Products of Herpes Simplex Virus Type 1 Gene UL47

The major tegument structural protein VP22 targets areas of dispersed nucleolin and marginalized chromatin during productive herpes simplex virus 1 infection

Phosphorylation of herpes simplex virus type 1 Us11 protein is independent of viral genome expression

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