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 (Academic Journal)peer-review

6 Citations (Scopus)


The UL14 gene product of herpes simplex virus is a 32kDa 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 degrees C, whereas it was obstructed by treatment with the microfilament-disrupting drug cytochalasin 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)357-63
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number3
Publication statusPublished - 1 Nov 2002


  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cercopithecus aethiops
  • Cytochalasin D
  • DNA Primers
  • Heat-Shock Response
  • Molecular Sequence Data
  • Mutation
  • Protein Transport
  • Sequence Deletion
  • Sequence Homology, Amino Acid
  • Vero Cells
  • Viral Proteins
  • Journal Article
  • Research Support, Non-U.S. Gov't


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