PMID- 14671124
OWN - NLM
STAT- MEDLINE
DCOM- 20040120
LR  - 20191210
IS  - 0022-538X (Print)
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Linking)
VI  - 78
IP  - 1
DP  - 2004 Jan
TI  - The Rep protein of adeno-associated virus type 2 interacts with single-stranded 
      DNA-binding proteins that enhance viral replication.
PG  - 441-53
AB  - Adeno-associated virus (AAV) type 2 is a human parvovirus whose replication is 
      dependent upon cellular proteins as well as functions supplied by helper viruses. 
      The minimal herpes simplex virus type 1 (HSV-1) proteins that support AAV 
      replication in cell culture are the helicase-primase complex of UL5, UL8, and 
      UL52, together with the UL29 gene product ICP8. We show that AAV and HSV-1 
      replication proteins colocalize at discrete intranuclear sites. Transfections 
      with mutant genes demonstrate that enzymatic functions of the helicase-primase 
      are not essential. The ICP8 protein alone enhances AAV replication in an in vitro 
      assay. We also show localization of the cellular replication protein A (RPA) at 
      AAV centers under a variety of conditions that support replication. In vitro 
      assays demonstrate that the AAV Rep68 and Rep78 proteins interact with the 
      single-stranded DNA-binding proteins (ssDBPs) of Ad (Ad-DBP), HSV-1 (ICP8), and 
      the cell (RPA) and that these proteins enhance binding and nicking of Rep 
      proteins at the origin. These results highlight the importance of intranuclear 
      localization and suggest that Rep interaction with multiple ssDBPs allows AAV to 
      replicate under a diverse set of conditions.
FAU - Stracker, Travis H
AU  - Stracker TH
AD  - Laboratory of Genetics, The Salk Institute for Biological Studies, La Jolla, 
      California 92037, USA.
FAU - Cassell, Geoffrey D
AU  - Cassell GD
FAU - Ward, Peter
AU  - Ward P
FAU - Loo, Yueh-Ming
AU  - Loo YM
FAU - van Breukelen, Bas
AU  - van Breukelen B
FAU - Carrington-Lawrence, Stacy D
AU  - Carrington-Lawrence SD
FAU - Hamatake, Robert K
AU  - Hamatake RK
FAU - van der Vliet, Peter C
AU  - van der Vliet PC
FAU - Weller, Sandra K
AU  - Weller SK
FAU - Melendy, Thomas
AU  - Melendy T
FAU - Weitzman, Matthew D
AU  - Weitzman MD
LA  - eng
GR  - R01 AI051686/AI/NIAID NIH HHS/United States
GR  - R37 AI021747/AI/NIAID NIH HHS/United States
GR  - AI43341/AI/NIAID NIH HHS/United States
GR  - GM56406/GM/NIGMS NIH HHS/United States
GR  - AI01686/AI/NIAID NIH HHS/United States
GR  - R01 AI021747/AI/NIAID NIH HHS/United States
GR  - R29 GM056406/GM/NIGMS NIH HHS/United States
GR  - AI51686/AI/NIAID NIH HHS/United States
GR  - AI21747/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (DNA, Single-Stranded)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (ICP8 protein, Simplexvirus)
RN  - 0 (Viral Proteins)
RN  - 137750-19-7 (rep proteins, Adeno-associated virus 2)
SB  - IM
MH  - Animals
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - DNA, Single-Stranded/*metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Dependovirus/genetics/metabolism/*physiology
MH  - HeLa Cells
MH  - Herpesvirus 1, Human/genetics/physiology
MH  - Humans
MH  - Transfection
MH  - Vero Cells
MH  - Viral Proteins/*metabolism
MH  - *Virus Replication
PMC - PMC303412
EDAT- 2003/12/13 05:00
MHDA- 2004/01/21 05:00
PMCR- 2004/01/01
CRDT- 2003/12/13 05:00
PHST- 2003/12/13 05:00 [pubmed]
PHST- 2004/01/21 05:00 [medline]
PHST- 2003/12/13 05:00 [entrez]
PHST- 2004/01/01 00:00 [pmc-release]
AID - 1448 [pii]
AID - 10.1128/jvi.78.1.441-453.2004 [doi]
PST - ppublish
SO  - J Virol. 2004 Jan;78(1):441-53. doi: 10.1128/jvi.78.1.441-453.2004.