Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins

Yohei Yamauchi, Fumi Goshima, Tetsushi Yoshikawa, Naoki Nozawa, Tetsuo Koshizuka, Yukihiro Nishiyama

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The UL14 gene product of herpes simplex virus is a 32 kDa protein expressed late in infection and is a minor component of the virion tegument. We recently showed that the wild-type UL14 protein has heat shock protein (HSP)-like and/or molecular chaperone-like functions. In this study, the intracellular localization of UL14 wild-type and deletion mutant proteins was examined in transfected cells by immunofluorescence. We found that N-terminus deleted but not wild-type/C-terminus deleted mutant proteins showed a significant number of cytoplasmic, multi-cellular stains in transfected Vero cells. The effect was greatly intensified by subjecting cells to heat shock at 43°C, whereas it was obstructed by treatment with the microfilament-disrupting drug cytochalas in D. The staining patterns of UL14 antigen-positive cells after heat shock suggested a cell-to-cell spread of the protein. Although the mechanism is unclear, the phenomenon seems to be an unprecedented type of intercellular trafficking.

Original languageEnglish
Pages (from-to)357-363
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume298
Issue number3
DOIs
Publication statusPublished - 01-01-2002
Externally publishedYes

Fingerprint

Human Herpesvirus 2
Mutant Proteins
Viruses
Proteins
Molecular Chaperones
Heat-Shock Proteins
Shock
Hot Temperature
Coloring Agents
Genes
Cells
Vero Cells
Antigens
Simplexvirus
Actin Cytoskeleton
Virion
Fluorescent Antibody Technique
Pharmaceutical Preparations
Staining and Labeling
Infection

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Yamauchi, Yohei ; Goshima, Fumi ; Yoshikawa, Tetsushi ; Nozawa, Naoki ; Koshizuka, Tetsuo ; Nishiyama, Yukihiro. / Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins. In: Biochemical and Biophysical Research Communications. 2002 ; Vol. 298, No. 3. pp. 357-363.
@article{4a159d448089464bae05be38dc148c15,
title = "Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins",
abstract = "The UL14 gene product of herpes simplex virus is a 32 kDa protein expressed late in infection and is a minor component of the virion tegument. We recently showed that the wild-type UL14 protein has heat shock protein (HSP)-like and/or molecular chaperone-like functions. In this study, the intracellular localization of UL14 wild-type and deletion mutant proteins was examined in transfected cells by immunofluorescence. We found that N-terminus deleted but not wild-type/C-terminus deleted mutant proteins showed a significant number of cytoplasmic, multi-cellular stains in transfected Vero cells. The effect was greatly intensified by subjecting cells to heat shock at 43°C, whereas it was obstructed by treatment with the microfilament-disrupting drug cytochalas in D. The staining patterns of UL14 antigen-positive cells after heat shock suggested a cell-to-cell spread of the protein. Although the mechanism is unclear, the phenomenon seems to be an unprecedented type of intercellular trafficking.",
author = "Yohei Yamauchi and Fumi Goshima and Tetsushi Yoshikawa and Naoki Nozawa and Tetsuo Koshizuka and Yukihiro Nishiyama",
year = "2002",
month = "1",
day = "1",
doi = "10.1016/S0006-291X(02)02452-X",
language = "English",
volume = "298",
pages = "357--363",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "3",

}

Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins. / Yamauchi, Yohei; Goshima, Fumi; Yoshikawa, Tetsushi; Nozawa, Naoki; Koshizuka, Tetsuo; Nishiyama, Yukihiro.

In: Biochemical and Biophysical Research Communications, Vol. 298, No. 3, 01.01.2002, p. 357-363.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Intercellular trafficking of herpes simplex virus type 2 UL14 deletion mutant proteins

AU - Yamauchi, Yohei

AU - Goshima, Fumi

AU - Yoshikawa, Tetsushi

AU - Nozawa, Naoki

AU - Koshizuka, Tetsuo

AU - Nishiyama, Yukihiro

PY - 2002/1/1

Y1 - 2002/1/1

N2 - The UL14 gene product of herpes simplex virus is a 32 kDa protein expressed late in infection and is a minor component of the virion tegument. We recently showed that the wild-type UL14 protein has heat shock protein (HSP)-like and/or molecular chaperone-like functions. In this study, the intracellular localization of UL14 wild-type and deletion mutant proteins was examined in transfected cells by immunofluorescence. We found that N-terminus deleted but not wild-type/C-terminus deleted mutant proteins showed a significant number of cytoplasmic, multi-cellular stains in transfected Vero cells. The effect was greatly intensified by subjecting cells to heat shock at 43°C, whereas it was obstructed by treatment with the microfilament-disrupting drug cytochalas in D. The staining patterns of UL14 antigen-positive cells after heat shock suggested a cell-to-cell spread of the protein. Although the mechanism is unclear, the phenomenon seems to be an unprecedented type of intercellular trafficking.

AB - The UL14 gene product of herpes simplex virus is a 32 kDa protein expressed late in infection and is a minor component of the virion tegument. We recently showed that the wild-type UL14 protein has heat shock protein (HSP)-like and/or molecular chaperone-like functions. In this study, the intracellular localization of UL14 wild-type and deletion mutant proteins was examined in transfected cells by immunofluorescence. We found that N-terminus deleted but not wild-type/C-terminus deleted mutant proteins showed a significant number of cytoplasmic, multi-cellular stains in transfected Vero cells. The effect was greatly intensified by subjecting cells to heat shock at 43°C, whereas it was obstructed by treatment with the microfilament-disrupting drug cytochalas in D. The staining patterns of UL14 antigen-positive cells after heat shock suggested a cell-to-cell spread of the protein. Although the mechanism is unclear, the phenomenon seems to be an unprecedented type of intercellular trafficking.

UR - http://www.scopus.com/inward/record.url?scp=0036430412&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036430412&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(02)02452-X

DO - 10.1016/S0006-291X(02)02452-X

M3 - Article

C2 - 12413948

AN - SCOPUS:0036430412

VL - 298

SP - 357

EP - 363

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 3

ER -