PMID- 10233977
OWN - NLM
STAT- MEDLINE
DCOM- 19990607
LR  - 20200724
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 73
IP  - 6
DP  - 1999 Jun
TI  - Viral immediate-early proteins abrogate the modification by SUMO-1 of PML and
      Sp100 proteins, correlating with nuclear body disruption.
PG  - 5137-43
AB  - PML nuclear bodies (NBs) are subnuclear structures whose integrity is compromised
      in certain human diseases, including leukemia and neurodegenerative disorders.
      Infection by a number of DNA viruses similarly triggers the reorganization of
      these structures, suggesting an important role for the NBs in the viral infection
      process. While expression of the adenovirus E4 ORF3 protein leads to only a
      moderate redistribution of PML to filamentous structures, the herpes simplex
      virus (HSV) ICP0 protein and the cytomegalovirus (CMV) IE1 protein both induce a 
      complete disruption of the NB structure. Recently, we and others have shown that 
      the NB proteins PML and Sp100 are posttranslationally modified by covalent
      linkage with the ubiquitin-related SUMO-1 protein and that this modification may 
      promote the assembly of these structures. Here we show that the HSV ICP0 and CMV 
      IE1 proteins specifically abrogate the SUMO-1 modification of PML and Sp100,
      whereas the adenovirus E4 ORF3 protein does not affect this process. The
      potential of ICP0 and IE1 to alter SUMO-1 modification is directly linked to
      their capacity to disassemble NBs, thus strengthening the role for SUMO-1
      conjugation in maintenance of the structural integrity of the NBs. This
      observation supports a model in which ICP0 and IE1 disrupt the NBs either by
      preventing the formation or by degrading of the SUMO-1-modified PML and Sp100
      protein species. Finally, we show that the IE1 protein itself is a substrate for 
      SUMO-1 modification, thus representing the first viral protein found to undergo
      this new type of posttranslational modification.
FAU - Muller, S
AU  - Muller S
AD  - Unite de Recombinaison et Expression Genetique, INSERM U 163, Institut Pasteur,
      28 rue du Dr. Roux, 75724 Paris Cedex 15, France.
FAU - Dejean, A
AU  - Dejean A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (Antigens, Nuclear)
RN  - 0 (Autoantigens)
RN  - 0 (IE1 protein, cytomegalovirus)
RN  - 0 (Immediate-Early Proteins)
RN  - 0 (Neoplasm Proteins)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Promyelocytic Leukemia Protein)
RN  - 0 (SUMO-1 Protein)
RN  - 0 (Transcription Factors)
RN  - 0 (Tumor Suppressor Proteins)
RN  - 0 (Ubiquitins)
RN  - 0 (Viral Proteins)
RN  - 135844-47-2 (Sp100 protein, human)
RN  - 143220-95-5 (PML protein, human)
RN  - EC 2.3.2.27 (Ubiquitin-Protein Ligases)
RN  - EC 2.3.2.27 (Vmw110 protein, Human herpesvirus 1)
SB  - IM
MH  - *Antigens, Nuclear
MH  - Autoantigens/*physiology
MH  - Humans
MH  - Immediate-Early Proteins/*physiology
MH  - Neoplasm Proteins/*physiology
MH  - Nuclear Matrix/*chemistry
MH  - Nuclear Proteins/*physiology
MH  - Promyelocytic Leukemia Protein
MH  - Protein Processing, Post-Translational
MH  - SUMO-1 Protein
MH  - Transcription Factors/*physiology
MH  - Tumor Suppressor Proteins
MH  - Ubiquitin-Protein Ligases
MH  - Ubiquitins/*physiology
MH  - *Viral Proteins
PMC - PMC112559
EDAT- 1999/05/11 00:00
MHDA- 1999/05/11 00:01
CRDT- 1999/05/11 00:00
PHST- 1999/05/11 00:00 [pubmed]
PHST- 1999/05/11 00:01 [medline]
PHST- 1999/05/11 00:00 [entrez]
AID - 10.1128/JVI.73.6.5137-5143.1999 [doi]
PST - ppublish
SO  - J Virol. 1999 Jun;73(6):5137-43. doi: 10.1128/JVI.73.6.5137-5143.1999.