Identification and characterization of the UL7 gene product of herpes simplex virus type 2

Naoki Nozawa, Tohru Daikoku, Yohei Yamauchi, Hiroki Takakuwa, Fumi Goshima, Tetsushi Yoshikawa, Yukihiro Nishiyama

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

We have raised a rabbit polyclonal antiserum against a recombinant 6× His-tagged herpes simplex virus type 2 (HSV-2) UL7 fusion protein expressed in Escherichia coli. The antiserum specifically reacted with a 33 kDa protein in HSV-1 and HSV-2-infected cell lysates, and was used to characterize the UL7 gene product of HSV-2. The UL7 protein was produced in the late phase of infection, and its synthesis was highly inhibited, but not abolished by the addition of acyclovir (ACV). The UL7 protein associated with extracellular virions and also with all types of capsids, including A, B, and C capsids, though the association seemed to be weak. Indirect immunofluorescence studies revealed that at 9 h postinfection, UL7 specific fluorescence was detected in part or all of the nucleus, and the specific fluorescence colocalized with the scaffold protein ICP35. However, at later times postinfection, the UL7 protein was mainly detected as a mass in a juxtanuclear cytoplasmic region. In addition, transmission immunoelectron microscopy (TIEM) confirmed the association of the UL7 protein with intracellular capsids and virions in HSV-2-infected cells. The HSV-2 UL7 protein contained a domain highly conserved in all herpesviruses, part of which exhibited a homology with domains in the fission yeast Schizosaccharomyces pombe DNA topoisomerase III. We discuss the possibility that the UL7 protein may play a supplementary role in the viral DNA cleavage/packaging process.

Original languageEnglish
Pages (from-to)257-266
Number of pages10
JournalVirus Genes
Volume24
Issue number3
DOIs
Publication statusPublished - 20-06-2002

Fingerprint

Human Herpesvirus 2
Genes
Proteins
Capsid
His-His-His-His-His-His
Schizosaccharomyces
Virion
Immune Sera
Fluorescence
DNA Packaging
DNA Cleavage
Immunoelectron Microscopy
Acyclovir
Herpesviridae
Viral DNA
Human Herpesvirus 1
Indirect Fluorescent Antibody Technique
Escherichia coli
Rabbits

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics
  • Virology

Cite this

Nozawa, N., Daikoku, T., Yamauchi, Y., Takakuwa, H., Goshima, F., Yoshikawa, T., & Nishiyama, Y. (2002). Identification and characterization of the UL7 gene product of herpes simplex virus type 2. Virus Genes, 24(3), 257-266. https://doi.org/10.1023/A:1015332716927
Nozawa, Naoki ; Daikoku, Tohru ; Yamauchi, Yohei ; Takakuwa, Hiroki ; Goshima, Fumi ; Yoshikawa, Tetsushi ; Nishiyama, Yukihiro. / Identification and characterization of the UL7 gene product of herpes simplex virus type 2. In: Virus Genes. 2002 ; Vol. 24, No. 3. pp. 257-266.
@article{b9db80c1767646868a91682a53b6ecd1,
title = "Identification and characterization of the UL7 gene product of herpes simplex virus type 2",
abstract = "We have raised a rabbit polyclonal antiserum against a recombinant 6× His-tagged herpes simplex virus type 2 (HSV-2) UL7 fusion protein expressed in Escherichia coli. The antiserum specifically reacted with a 33 kDa protein in HSV-1 and HSV-2-infected cell lysates, and was used to characterize the UL7 gene product of HSV-2. The UL7 protein was produced in the late phase of infection, and its synthesis was highly inhibited, but not abolished by the addition of acyclovir (ACV). The UL7 protein associated with extracellular virions and also with all types of capsids, including A, B, and C capsids, though the association seemed to be weak. Indirect immunofluorescence studies revealed that at 9 h postinfection, UL7 specific fluorescence was detected in part or all of the nucleus, and the specific fluorescence colocalized with the scaffold protein ICP35. However, at later times postinfection, the UL7 protein was mainly detected as a mass in a juxtanuclear cytoplasmic region. In addition, transmission immunoelectron microscopy (TIEM) confirmed the association of the UL7 protein with intracellular capsids and virions in HSV-2-infected cells. The HSV-2 UL7 protein contained a domain highly conserved in all herpesviruses, part of which exhibited a homology with domains in the fission yeast Schizosaccharomyces pombe DNA topoisomerase III. We discuss the possibility that the UL7 protein may play a supplementary role in the viral DNA cleavage/packaging process.",
author = "Naoki Nozawa and Tohru Daikoku and Yohei Yamauchi and Hiroki Takakuwa and Fumi Goshima and Tetsushi Yoshikawa and Yukihiro Nishiyama",
year = "2002",
month = "6",
day = "20",
doi = "10.1023/A:1015332716927",
language = "English",
volume = "24",
pages = "257--266",
journal = "Virus Genes",
issn = "0920-8569",
publisher = "Springer Netherlands",
number = "3",

}

Nozawa, N, Daikoku, T, Yamauchi, Y, Takakuwa, H, Goshima, F, Yoshikawa, T & Nishiyama, Y 2002, 'Identification and characterization of the UL7 gene product of herpes simplex virus type 2', Virus Genes, vol. 24, no. 3, pp. 257-266. https://doi.org/10.1023/A:1015332716927

Identification and characterization of the UL7 gene product of herpes simplex virus type 2. / Nozawa, Naoki; Daikoku, Tohru; Yamauchi, Yohei; Takakuwa, Hiroki; Goshima, Fumi; Yoshikawa, Tetsushi; Nishiyama, Yukihiro.

In: Virus Genes, Vol. 24, No. 3, 20.06.2002, p. 257-266.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Identification and characterization of the UL7 gene product of herpes simplex virus type 2

AU - Nozawa, Naoki

AU - Daikoku, Tohru

AU - Yamauchi, Yohei

AU - Takakuwa, Hiroki

AU - Goshima, Fumi

AU - Yoshikawa, Tetsushi

AU - Nishiyama, Yukihiro

PY - 2002/6/20

Y1 - 2002/6/20

N2 - We have raised a rabbit polyclonal antiserum against a recombinant 6× His-tagged herpes simplex virus type 2 (HSV-2) UL7 fusion protein expressed in Escherichia coli. The antiserum specifically reacted with a 33 kDa protein in HSV-1 and HSV-2-infected cell lysates, and was used to characterize the UL7 gene product of HSV-2. The UL7 protein was produced in the late phase of infection, and its synthesis was highly inhibited, but not abolished by the addition of acyclovir (ACV). The UL7 protein associated with extracellular virions and also with all types of capsids, including A, B, and C capsids, though the association seemed to be weak. Indirect immunofluorescence studies revealed that at 9 h postinfection, UL7 specific fluorescence was detected in part or all of the nucleus, and the specific fluorescence colocalized with the scaffold protein ICP35. However, at later times postinfection, the UL7 protein was mainly detected as a mass in a juxtanuclear cytoplasmic region. In addition, transmission immunoelectron microscopy (TIEM) confirmed the association of the UL7 protein with intracellular capsids and virions in HSV-2-infected cells. The HSV-2 UL7 protein contained a domain highly conserved in all herpesviruses, part of which exhibited a homology with domains in the fission yeast Schizosaccharomyces pombe DNA topoisomerase III. We discuss the possibility that the UL7 protein may play a supplementary role in the viral DNA cleavage/packaging process.

AB - We have raised a rabbit polyclonal antiserum against a recombinant 6× His-tagged herpes simplex virus type 2 (HSV-2) UL7 fusion protein expressed in Escherichia coli. The antiserum specifically reacted with a 33 kDa protein in HSV-1 and HSV-2-infected cell lysates, and was used to characterize the UL7 gene product of HSV-2. The UL7 protein was produced in the late phase of infection, and its synthesis was highly inhibited, but not abolished by the addition of acyclovir (ACV). The UL7 protein associated with extracellular virions and also with all types of capsids, including A, B, and C capsids, though the association seemed to be weak. Indirect immunofluorescence studies revealed that at 9 h postinfection, UL7 specific fluorescence was detected in part or all of the nucleus, and the specific fluorescence colocalized with the scaffold protein ICP35. However, at later times postinfection, the UL7 protein was mainly detected as a mass in a juxtanuclear cytoplasmic region. In addition, transmission immunoelectron microscopy (TIEM) confirmed the association of the UL7 protein with intracellular capsids and virions in HSV-2-infected cells. The HSV-2 UL7 protein contained a domain highly conserved in all herpesviruses, part of which exhibited a homology with domains in the fission yeast Schizosaccharomyces pombe DNA topoisomerase III. We discuss the possibility that the UL7 protein may play a supplementary role in the viral DNA cleavage/packaging process.

UR - http://www.scopus.com/inward/record.url?scp=0035988850&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035988850&partnerID=8YFLogxK

U2 - 10.1023/A:1015332716927

DO - 10.1023/A:1015332716927

M3 - Article

C2 - 12086147

AN - SCOPUS:0035988850

VL - 24

SP - 257

EP - 266

JO - Virus Genes

JF - Virus Genes

SN - 0920-8569

IS - 3

ER -