PMID- 15166453
OWN - NLM
STAT- MEDLINE
DCOM- 20040624
LR  - 20200303
IS  - 0022-1317 (Print)
IS  - 0022-1317 (Linking)
VI  - 85
IP  - Pt 6
DP  - 2004 Jun
TI  - Ser-123 of the large antigen of hepatitis delta virus modulates its cellular 
      localization to the nucleolus, SC-35 speckles or the cytoplasm.
PG  - 1685-1694
LID - 10.1099/vir.0.19690-0 [doi]
AB  - Hepatitis delta virus (HDV) is a defective virus and requires hepatitis B virus 
      (HBV) to supply envelope proteins (HBsAg) for maturation and secretion. It is 
      known that two proteins produced by HDV, the small (SDAg) and large (LDAg) 
      antigens, are located in the nucleolus, speckles and the cytoplasm and are 
      involved in genome replication and virion packaging. However, little is known 
      about how they are targeted to the specific sites where they act. A green 
      fluorescence protein fused to LDAg (GFP-LD) has been shown previously to 
      translocate from the nucleolus to SC-35 speckles in the presence of the casein 
      kinase II inhibitor dichlororibofuranosyl benzimidazole. In this study, we 
      determined which amino acids of GFP-LD were responsible for the translocation 
      from the nucleolus to SC-35 speckles and created three GFP-LD derivatives, 
      GFP-LDS2A, GFP-LDS123A and GFP-LDS2/123A. Fluorescence microscopy studies showed 
      that Ser-123 mutants had a high tendency to target SC-35 speckles in both 
      transfected HeLa and HuH-7 cells and suggested that Ser-123, but not Ser-2, plays 
      a role in modulating LDAg translocation to the nucleolus or to SC-35 speckles. 
      This study also demonstrated that HBsAg plays a role in facilitating the 
      transportation of LDAg from the nucleus to cytoplasm. Compared with GFP-LD and 
      GFP-LDS2A, mutants of Ser-123 were less efficiently transported to the cytoplasm 
      and resulted in a lower level of secretion. In contrast, little or no 
      isoprenylation mutant was observed in the cytoplasm of HuH-7 cells expressing 
      HbsAg, suggesting that the isoprenylation of LDAg plays a role in export from the 
      nucleus. Thus, the current study demonstrated that both cis and trans elements 
      modulate HDAg translocation to various subcellular sites.
FAU - Tan, Keng-Poo
AU  - Tan KP
AD  - Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, 
      Taiwan 112.
FAU - Shih, Ko-Nien
AU  - Shih KN
AD  - Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, 
      Taiwan 112.
FAU - Lo, Szecheng J
AU  - Lo SJ
AD  - Department of Life Science, School of Medicine, Chang Gung University, TaoYun, 
      Taiwan 333.
AD  - Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, 
      Taiwan 112.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - J Gen Virol
JT  - The Journal of general virology
JID - 0077340
RN  - 0 (Hepatitis B Surface Antigens)
RN  - 0 (Hepatitis delta Antigens)
RN  - 0 (Luminescent Proteins)
RN  - 147336-22-9 (Green Fluorescent Proteins)
RN  - 452VLY9402 (Serine)
SB  - IM
MH  - Active Transport, Cell Nucleus
MH  - Cell Nucleolus/*metabolism
MH  - Cytoplasm/*metabolism
MH  - Green Fluorescent Proteins
MH  - HeLa Cells
MH  - Hepatitis B Surface Antigens/metabolism
MH  - Hepatitis Delta Virus/*immunology
MH  - Hepatitis delta Antigens/chemistry/*metabolism
MH  - Humans
MH  - Luminescent Proteins/metabolism
MH  - Protein Transport
MH  - Serine
MH  - Transfection
EDAT- 2004/05/29 05:00
MHDA- 2004/06/25 05:00
CRDT- 2004/05/29 05:00
PHST- 2004/05/29 05:00 [pubmed]
PHST- 2004/06/25 05:00 [medline]
PHST- 2004/05/29 05:00 [entrez]
AID - 10.1099/vir.0.19690-0 [doi]
PST - ppublish
SO  - J Gen Virol. 2004 Jun;85(Pt 6):1685-1694. doi: 10.1099/vir.0.19690-0.