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Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells.

Abstract The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by HIV-1 infected brain macrophages. Several steps of viral replication, including assembly and budding, differ between macrophages and T cells; it is likely that cell-specific host factors mediate these differences. We previously defined Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent membrane-binding protein that can aggregate phospholipid-containing lipid rafts, is expressed to high levels in macrophages, but not in T lymphocytes or the 293T cell line. Here, we use bimolecular fluorescence complementation in the 293T cell model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells increases Gag processing and HIV-1 production. These data provide new evidence that Anx2, by interacting with Gag at the membranes that support viral assembly, functions in the late stages of HIV-1 replication.
PMID
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Authors

Mayor MeshTerms

Phosphatidylinositol 4,5-Diphosphate

Virus Replication

Keywords
Journal Title plos one
Publication Year Start
%A Harrist, Alexia V.; Ryzhova, Elena V.; Harvey, Thomas; Gonz?lez-Scarano, Francisco
%T Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells.
%J PloS one, vol. 4, no. 3, p. e5020
%D 03/2009
%V 4
%N 3
%M eng
%B The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by HIV-1 infected brain macrophages. Several steps of viral replication, including assembly and budding, differ between macrophages and T cells; it is likely that cell-specific host factors mediate these differences. We previously defined Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent membrane-binding protein that can aggregate phospholipid-containing lipid rafts, is expressed to high levels in macrophages, but not in T lymphocytes or the 293T cell line. Here, we use bimolecular fluorescence complementation in the 293T cell model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells increases Gag processing and HIV-1 production. These data provide new evidence that Anx2, by interacting with Gag at the membranes that support viral assembly, functions in the late stages of HIV-1 replication.
%K Annexin A2, Cell Line, HIV-1, Human Immunodeficiency Virus Proteins, Humans, Membrane Microdomains, Phosphatidylinositol 4,5-Diphosphate, Virus Replication, gag Gene Products, Human Immunodeficiency Virus
%P e5020
%Y 10.1371/journal.pone.0005020
%W PHY
%G AUTHOR
%R 2009PLoSO...4....0H

@Article{Harrist2009,
author="Harrist, Alexia V.
and Ryzhova, Elena V.
and Harvey, Thomas
and Gonz{\'a}lez-Scarano, Francisco",
title="Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells.",
journal="PloS one",
year="2009",
month="Mar",
day="27",
volume="4",
number="3",
pages="e5020",
keywords="Annexin A2",
keywords="Cell Line",
keywords="HIV-1",
keywords="Human Immunodeficiency Virus Proteins",
keywords="Humans",
keywords="Membrane Microdomains",
keywords="Phosphatidylinositol 4,5-Diphosphate",
keywords="Virus Replication",
keywords="gag Gene Products, Human Immunodeficiency Virus",
abstract="The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by HIV-1 infected brain macrophages. Several steps of viral replication, including assembly and budding, differ between macrophages and T cells; it is likely that cell-specific host factors mediate these differences. We previously defined Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent membrane-binding protein that can aggregate phospholipid-containing lipid rafts, is expressed to high levels in macrophages, but not in T lymphocytes or the 293T cell line. Here, we use bimolecular fluorescence complementation in the 293T cell model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells increases Gag processing and HIV-1 production. These data provide new evidence that Anx2, by interacting with Gag at the membranes that support viral assembly, functions in the late stages of HIV-1 replication.",
issn="1932-6203",
doi="10.1371/journal.pone.0005020",
url="http://www.ncbi.nlm.nih.gov/pubmed/19325895",
language="eng"
}

%0 Journal Article
%T Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells.
%A Harrist, Alexia V.
%A Ryzhova, Elena V.
%A Harvey, Thomas
%A Gonz?lez-Scarano, Francisco
%J PloS one
%D 2009
%8 March 27
%V 4
%N 3
%@ 1932-6203
%G eng
%F Harrist2009
%X The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by HIV-1 infected brain macrophages. Several steps of viral replication, including assembly and budding, differ between macrophages and T cells; it is likely that cell-specific host factors mediate these differences. We previously defined Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent membrane-binding protein that can aggregate phospholipid-containing lipid rafts, is expressed to high levels in macrophages, but not in T lymphocytes or the 293T cell line. Here, we use bimolecular fluorescence complementation in the 293T cell model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells increases Gag processing and HIV-1 production. These data provide new evidence that Anx2, by interacting with Gag at the membranes that support viral assembly, functions in the late stages of HIV-1 replication.
%K Annexin A2
%K Cell Line
%K HIV-1
%K Human Immunodeficiency Virus Proteins
%K Humans
%K Membrane Microdomains
%K Phosphatidylinositol 4,5-Diphosphate
%K Virus Replication
%K gag Gene Products, Human Immunodeficiency Virus
%U http://dx.doi.org/10.1371/journal.pone.0005020
%U http://www.ncbi.nlm.nih.gov/pubmed/19325895
%P e5020

PT Journal
AU Harrist, AV
   Ryzhova, EV
   Harvey, T
   Gonz?lez-Scarano, F
TI Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells.
SO PloS one
JI PLoS ONE
PD 03
PY 2009
BP e5020
VL 4
IS 3
DI 10.1371/journal.pone.0005020
LA eng
DE Annexin A2; Cell Line; HIV-1; Human Immunodeficiency Virus Proteins; Humans; Membrane Microdomains; Phosphatidylinositol 4,5-Diphosphate; Virus Replication; gag Gene Products, Human Immunodeficiency Virus
AB The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by HIV-1 infected brain macrophages. Several steps of viral replication, including assembly and budding, differ between macrophages and T cells; it is likely that cell-specific host factors mediate these differences. We previously defined Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent membrane-binding protein that can aggregate phospholipid-containing lipid rafts, is expressed to high levels in macrophages, but not in T lymphocytes or the 293T cell line. Here, we use bimolecular fluorescence complementation in the 293T cell model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells increases Gag processing and HIV-1 production. These data provide new evidence that Anx2, by interacting with Gag at the membranes that support viral assembly, functions in the late stages of HIV-1 replication.
ER

PMID- 19325895
OWN - NLM
STAT- MEDLINE
DA  - 20090327
DCOM- 20090701
LR  - 20141210
IS  - 1932-6203 (Electronic)
IS  - 1932-6203 (Linking)
VI  - 4
IP  - 3
DP  - 2009
TI  - Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5)
      bisphosphate-containing lipid rafts and increases viral production in 293T cells.
PG  - e5020
LID - 10.1371/journal.pone.0005020 [doi]
AB  - The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by
      HIV-1 infected brain macrophages. Several steps of viral replication, including
      assembly and budding, differ between macrophages and T cells; it is likely that
      cell-specific host factors mediate these differences. We previously defined
      Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived
      macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent
      membrane-binding protein that can aggregate phospholipid-containing lipid rafts, 
      is expressed to high levels in macrophages, but not in T lymphocytes or the 293T 
      cell line. Here, we use bimolecular fluorescence complementation in the 293T cell
      model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol
      (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates
      viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells
      increases Gag processing and HIV-1 production. These data provide new evidence
      that Anx2, by interacting with Gag at the membranes that support viral assembly, 
      functions in the late stages of HIV-1 replication.
FAU - Harrist, Alexia V
AU  - Harrist AV
AD  - Department of Neurology and Microbiology, University of Pennsylvania,
      Philadelphia, PA, USA.
FAU - Ryzhova, Elena V
AU  - Ryzhova EV
FAU - Harvey, Thomas
AU  - Harvey T
FAU - Gonzalez-Scarano, Francisco
AU  - Gonzalez-Scarano F
LA  - eng
GR  - F30 NS055523/NS/NINDS NIH HHS/United States
GR  - NS-27405/NS/NINDS NIH HHS/United States
GR  - P30 AI 045008/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20090327
PL  - United States
TA  - PLoS One
JT  - PloS one
JID - 101285081
RN  - 0 (ANXA2 protein, human)
RN  - 0 (Annexin A2)
RN  - 0 (Human Immunodeficiency Virus Proteins)
RN  - 0 (Phosphatidylinositol 4,5-Diphosphate)
RN  - 0 (gag Gene Products, Human Immunodeficiency Virus)
SB  - IM
MH  - Annexin A2/*metabolism
MH  - Cell Line
MH  - HIV-1/physiology
MH  - Human Immunodeficiency Virus Proteins/metabolism/physiology
MH  - Humans
MH  - Membrane Microdomains/chemistry/*metabolism
MH  - *Phosphatidylinositol 4,5-Diphosphate
MH  - *Virus Replication
MH  - gag Gene Products, Human Immunodeficiency Virus/*metabolism/physiology
PMC - PMC2657825
OID - NLM: PMC2657825
EDAT- 2009/03/28 09:00
MHDA- 2009/07/02 09:00
CRDT- 2009/03/28 09:00
PHST- 2008/11/14 [received]
PHST- 2009/02/24 [accepted]
PHST- 2009/03/27 [epublish]
AID - 10.1371/journal.pone.0005020 [doi]
PST - ppublish
SO  - PLoS One. 2009;4(3):e5020. doi: 10.1371/journal.pone.0005020. Epub 2009 Mar 27.
TY  - JOUR
AU  - Harrist, Alexia V.
AU  - Ryzhova, Elena V.
AU  - Harvey, Thomas
AU  - Gonz?lez-Scarano, Francisco
PY  - 2009/03/27
TI  - Anx2 interacts with HIV-1 Gag at phosphatidylinositol (4,5) bisphosphate-containing lipid rafts and increases viral production in 293T cells.
T2  - PLoS ONE
JO  - PloS one
SP  - e5020
VL  - 4
IS  - 3
KW  - Annexin A2
KW  - Cell Line
KW  - HIV-1
KW  - Human Immunodeficiency Virus Proteins
KW  - Humans
KW  - Membrane Microdomains
KW  - Phosphatidylinositol 4,5-Diphosphate
KW  - Virus Replication
KW  - gag Gene Products, Human Immunodeficiency Virus
N2  - The neuronal damage characteristic of HIV-1-mediated CNS diseases is inflicted by HIV-1 infected brain macrophages. Several steps of viral replication, including assembly and budding, differ between macrophages and T cells; it is likely that cell-specific host factors mediate these differences. We previously defined Annexin 2 (Anx2) as an HIV Gag binding partner in human monocyte-derived macrophages (MDMs) that promotes proper viral assembly. Anx2, a calcium-dependent membrane-binding protein that can aggregate phospholipid-containing lipid rafts, is expressed to high levels in macrophages, but not in T lymphocytes or the 293T cell line. Here, we use bimolecular fluorescence complementation in the 293T cell model to demonstrate that Anx2 and HIV-1 Gag interact at the phosphatidylinositol (4,5) bisphosphate-containing lipid raft membrane domains at which Gag mediates viral assembly. Furthermore, we demonstrate that Anx2 expression in 293T cells increases Gag processing and HIV-1 production. These data provide new evidence that Anx2, by interacting with Gag at the membranes that support viral assembly, functions in the late stages of HIV-1 replication.
SN  - 1932-6203
UR  - http://dx.doi.org/10.1371/journal.pone.0005020
UR  - http://www.ncbi.nlm.nih.gov/pubmed/19325895
ID  - Harrist2009
ER  - 
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