Characterization of the UL55 gene product of herpes simplex virus type 2.

Yamada, Hayato; Jiang, Yue-Mei; Oshima, Syun-ichirou; Daikoku, T.; Yamashita, Yoshihisa; Tsurumi, Tatsuya; Nishiyama, Yukihiro

doi:10.1099/0022-1317-79-8-1989

Cited by 21 publications

(25 citation statements)

References 13 publications

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“…Hence, U L 7 was found in HSV-2 virions (70), while U L 23 was detected in KHSV and alcelaphine herpesvirus-1 virions (21,111). In contrast, U L 55 is seemingly absent from mature HSV-2 (103). The current report clearly shows that all four proteins constitute novel components of the virions.…”

Section: Discussionmentioning

confidence: 59%

Comprehensive Characterization of Extracellular Herpes Simplex Virus Type 1 Virions

Loret

Guay

Lippé

2008

J Virol

343

425

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The herpes simplex virus type 1 (HSV-1) genome is contained in a capsid wrapped by a complex tegument layer and an external envelope. The poorly defined tegument plays a critical role throughout the viral life cycle, including delivery of capsids to the nucleus, viral gene expression, capsid egress, and acquisition of the viral envelope. Current data suggest tegumentation is a dynamic and sequential process that starts in the nucleus and continues in the cytoplasm. Over two dozen proteins are assumed to be or are known to ultimately be added to virions as tegument, but its precise composition is currently unknown. Moreover, a comprehensive analysis of all proteins found in HSV-1 virions is still lacking. To better understand the implication of the tegument and host proteins incorporated into the virions, highly purified mature extracellular viruses were analyzed by mass spectrometry. Herpes simplex virus type 1 (HSV-1) is a multilayered particle composed of a DNA core surrounded by a capsid, a tegument, and finally an envelope. The tegument consists of several proteins that are critical for the virus. For instance, upon the virus' entry into the cell, the tegument likely directs the virus to the nucleus (20, 33, 52, 90). There, the U L 36 tegument protein anchors the capsid to the nuclear pore to enable viral DNA transfer into the nucleus (90). Three other teguments, namely, ICP0, ICP4, and U L 48 (VP16), then play an essential role in initiating viral transcription (24). Meanwhile, the U L 41 (VHS) tegument specifically degrades some mRNAs to the benefit of the virus (93, 94). During egress, passage of the newly assembled capsids across the two nuclear membranes relies on the U L 31 (tegument)/U L 34 (transmembrane protein) complex, as well as the U S 3 tegument (46,81). Interestingly, despite the involvement of all three proteins in nuclear viral egress, only U S 3 is found in mature virions (81).

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Section: Discussionmentioning

confidence: 59%

Comprehensive Characterization of Extracellular Herpes Simplex Virus Type 1 Virions

Loret

Guay

Lippé

2008

J Virol

343

425

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“…Thus, some laboratories clearly demonstrated that UL34 and UL31 were detected only at the nuclear membrane in HSV-1-infected cells and in cells cotransfected with a UL34-and UL31-expressing plasmid (61,62,65). In contrast, the others, including this laboratory, reported nucleoplasmic localization of UL34 and/or UL31, in addition to nuclear membrane localization, in cells infected with HSV-1 or HSV-2 and in cells transiently coexpressing UL31 and UL34 (8,66,67,73,74). Furthermore, the nucleoplasmic distribution of pseudorabies virus UL31 and UL34 homologues in infected cells has also been reported (19).…”

Section: Discussionmentioning

confidence: 89%

Herpes Simplex Virus 1-Encoded Protein Kinase UL13 Phosphorylates Viral Us3 Protein Kinase and Regulates Nuclear Localization of Viral Envelopment Factors UL34 and UL31

Kato

Yamamoto

Ohno

et al. 2006

J Virol

107

103

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UL13 and Us3 are protein kinases encoded by herpes simplex virus 1. We report here that Us3 is a physiological substrate for UL13 in infected cells, based on the following observations. (i) The electrophoretic mobility, in denaturing gels, of Us3 isoforms from Vero cells infected with wild-type virus was slower than that of isoforms from cells infected with a UL13 deletion mutant virus (⌬UL13). After treatment with phosphatase, the electrophoretic mobility of the Us3 isoforms from cells infected with wild-type virus changed, with one isoform migrating as fast as one of the Us3 isoforms from ⌬UL13-infected cells. (ii) A recombinant protein containing a domain of Us3 was phosphorylated by UL13 in vitro. (iii) The phenotype of ⌬UL13 resembles that of a recombinant virus lacking the Us3 gene (⌬Us3) with respect to localization of the viral envelopment factors UL34 and UL31, whose localization has been shown to be regulated by Us3. UL34 and UL31 are localized in a smooth pattern throughout the nuclei of cells infected with wild-type virus, whereas their localization in ⌬UL13-and ⌬Us3-infected cells appeared as nuclear punctate patterns. These results indicate that UL13 phosphorylates Us3 in infected cells and regulates UL34 and UL31 localization, either by phosphorylating Us3 or by a Us3-independent mechanism.Herpes simplex virus 1 (HSV-1) encodes at least three protein kinases, UL13, Us3, and UL39 (63). This report presents studies of the interaction between UL13 and Us3. The background for these studies is as follows.First, UL13 is a serine/threonine protein kinase that is packaged in the tegument, a virion structural component located between the nucleocapsid and the envelope (9,12,13,29,52,68). UL13 plays a role in viral replication in cell cultures, since UL13 deletion mutants exhibit impaired replication in some cell lines, including rabbit skin cells and baby hamster kidney (BHK) cells (10,45,56,57,70). Although the mechanism by which UL13 acts in HSV-1-infected cells remains unclear, infection of rabbit skin cells and BHK cells with UL13 deletion mutants reduces the expression levels of the ␣ protein ICP0 and a subset of ␥ proteins, including UL26, UL26.5, UL38, UL41, and Us11 (56), suggesting that UL13 is involved in viral-gene expression in infected cells. UL13 would also be expected to function in early postinfection events, since tegument proteins are, in general, released into the cytoplasm of newly infected cells. In agreement with this possibility, phosphorylation of a tegument protein by UL13 has been implicated in promoting tegument disassembly in vitro (40).Second, UL13 may function by phosphorylating specific viral and cellular proteins. Thus far, gI/gE, ICP0, ICP22, Us1.5, UL47, UL49, p60, elongation factor 1␦ (EF-1␦), casein kinase II␤ subunit, and RNA polymerase II have been reported to be putative substrates for UL13 (4,10,20,29,32,37,44,51,57,63). However, the biological significance of UL13-mediated phosphorylation in infected cells remains unclear. Since the UL13 amino acid sequence is conse...

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“…Bound primary antibodies were detected using horseradish peroxidase-linked sheep anti-rabbit immunoglobulin G (IgG) (Amersham) and ECL Western blotting detection reagents (Amersham). The specific antiserum for the UL31 protein was described previously (Yamada et al, 1998).…”

Section: Generation Of Polyclonal Antisera In Rabbitsmentioning

confidence: 99%

“…Plasmid pET28-US2 was transformed into E. coli strain BL21(DE3) (Novagen) which, following induction with IPTG, expressed large quantities of 6iHis-US2 fusion protein. Purification of the US2 fusion protein and immunization were done as described previously (Yamada et al, 1998). Both preimmune and immune antisera were extensively adsorbed against acetone powder of E. coli strain BL21(DE3) and uninfected Vero cells prior to use, as described by Harlow & Lane (1988).…”

Section: Generation Of Polyclonal Antisera In Rabbitsmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of the herpes simplex virus type 2 (HSV-2) US2 gene product and a US2-deficient HSV-2 mutant.

Jiang

Yamada

Goshima

et al. 1998

Journal of General Virology

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The herpes simplex virus type 2 (HSV-2) US2 gene product was identified by using a rabbit polyclonal antiserum raised against a recombinant 6iHis-US2 fusion protein expressed in Escherichia coli. The antiserum reacted specifically with a 39 kDa protein in HSV-2 strain 186-infected cell lysates. The protein was not detectable in the presence of the virus DNA synthesis inhibitor phosphonoacetic acid. Indirect immunofluorescence studies localized the US2 protein in the cytoplasm and as discrete granules at late times post-infection within and at the

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Characterization of the UL55 gene product of herpes simplex virus type 2.

Cited by 21 publications

References 13 publications

Comprehensive Characterization of Extracellular Herpes Simplex Virus Type 1 Virions

Comprehensive Characterization of Extracellular Herpes Simplex Virus Type 1 Virions

Herpes Simplex Virus 1-Encoded Protein Kinase UL13 Phosphorylates Viral Us3 Protein Kinase and Regulates Nuclear Localization of Viral Envelopment Factors UL34 and UL31

Characterization of the herpes simplex virus type 2 (HSV-2) US2 gene product and a US2-deficient HSV-2 mutant.

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