PMID- 20106923
OWN - NLM
STAT- MEDLINE
DCOM- 20100407
LR  - 20211020
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 84
IP  - 8
DP  - 2010 Apr
TI  - Inhibition of herpes simplex virus type 1 replication by adeno-associated virus 
      rep proteins depends on their combined DNA-binding and ATPase/helicase 
      activities.
PG  - 3808-24
LID - 10.1128/JVI.01503-09 [doi]
AB  - Adeno-associated virus (AAV) has previously been shown to inhibit the replication 
      of its helper virus herpes simplex virus type 1 (HSV-1), and the inhibitory 
      activity has been attributed to the expression of the AAV Rep proteins. In the 
      present study, we assessed the Rep activities required for inhibition of HSV-1 
      replication using a panel of wild-type and mutant Rep proteins lacking defined 
      domains and activities. We found that the inhibition of HSV-1 replication 
      required Rep DNA-binding and ATPase/helicase activities but not endonuclease 
      activity. The Rep activities required for inhibition of HSV-1 replication 
      precisely coincided with the activities that were responsible for induction of 
      cellular DNA damage and apoptosis, suggesting that these three processes are 
      closely linked. Notably, the presence of Rep induced the hyperphosphorylation of 
      a DNA damage marker, replication protein A (RPA), which has been reported not to 
      be normally hyperphosphorylated during HSV-1 infection and to be sequestered away 
      from HSV-1 replication compartments during infection. Finally, we demonstrate 
      that the execution of apoptosis is not required for inhibition of HSV-1 
      replication and that the hyperphosphorylation of RPA per se is not inhibitory for 
      HSV-1 replication, suggesting that these two processes are not directly 
      responsible for the inhibition of HSV-1 replication by Rep.
FAU - Glauser, Daniel L
AU  - Glauser DL
AD  - Institute of Virology, University of Zurich, Winterthurerstrasse 266a, CH-8057 
      Zurich, Switzerland.
FAU - Seyffert, Michael
AU  - Seyffert M
FAU - Strasser, Regina
AU  - Strasser R
FAU - Franchini, Marco
AU  - Franchini M
FAU - Laimbacher, Andrea S
AU  - Laimbacher AS
FAU - Dresch, Christiane
AU  - Dresch C
FAU - de Oliveira, Anna Paula
AU  - de Oliveira AP
FAU - Vogel, Rebecca
AU  - Vogel R
FAU - Buning, Hildegard
AU  - Buning H
FAU - Salvetti, Anna
AU  - Salvetti A
FAU - Ackermann, Mathias
AU  - Ackermann M
FAU - Fraefel, Cornel
AU  - Fraefel C
LA  - eng
GR  - P01 CA069246/CA/NCI NIH HHS/United States
GR  - CA69246/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20100127
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (DNA, Viral)
RN  - 0 (Trans-Activators)
RN  - 0 (Viral Proteins)
RN  - 0 (replication initiator protein)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.4.- (DNA Helicases)
SB  - IM
MH  - Adenosine Triphosphatases/*metabolism
MH  - Animals
MH  - Apoptosis
MH  - Chlorocebus aethiops
MH  - DNA Damage
MH  - DNA Helicases/*metabolism
MH  - DNA, Viral/metabolism
MH  - Dependovirus/growth & development/*physiology
MH  - Herpesvirus 1, Human/growth & development/*physiology
MH  - Phosphorylation
MH  - Sequence Deletion
MH  - Trans-Activators/*metabolism
MH  - Vero Cells
MH  - Viral Proteins/*metabolism
MH  - *Virus Replication
PMC - PMC2849494
EDAT- 2010/01/29 06:00
MHDA- 2010/04/08 06:00
PMCR- 2010/10/01
CRDT- 2010/01/29 06:00
PHST- 2010/01/29 06:00 [entrez]
PHST- 2010/01/29 06:00 [pubmed]
PHST- 2010/04/08 06:00 [medline]
PHST- 2010/10/01 00:00 [pmc-release]
AID - JVI.01503-09 [pii]
AID - 1503-09 [pii]
AID - 10.1128/JVI.01503-09 [doi]
PST - ppublish
SO  - J Virol. 2010 Apr;84(8):3808-24. doi: 10.1128/JVI.01503-09. Epub 2010 Jan 27.