Molecular determinants responsible for the subcellular localization of HSV-1 UL4 protein

Wei Wei Pan, Jing Long, Jun Ji Xing, Chun Fu Zheng

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


The function of the herpes simplex virus type 1 (HSV-1) UL4 protein is still elusive. Our objective is to investigate the subcellular transport mechanism of the UL4 protein. In this study, fluorescence microscopy was employed to investigate the subcellular localization of UL4 and characterize the transport mechanism in living cells. By constructing a series of deletion mutants fused with enhanced yellow fluorescent protein (EYFP), the nuclear export signals (NES) of UL4 were for the first time mapped to amino acid residues 178 to 186. In addition, the N-terminal 19 amino acids are identified to be required for the granule-like cytoplasmic pattern of UL4. Furthermore, the UL4 protein was demonstrated to be exported to the cytoplasm through the NES in a chromosomal region maintenance 1 (CRM1)-dependent manner involving RanGTP hydrolysis.

Original languageEnglish (US)
Pages (from-to)347-356
Number of pages10
JournalVirologica Sinica
Issue number5
StatePublished - Oct 2011


  • Chromosomal region maintenance 1 (CRM1)
  • Herpes simplex virus type 1 (HSV-1)
  • Nuclear export signal (NES)
  • Subcellular localization
  • UL4

ASJC Scopus subject areas

  • Immunology
  • Molecular Medicine
  • Virology


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