Evidence map›Paper›PMID 19324886›Full record

ArticleThe Journal of biological chemistry2009

Inhibition of HIV-1 infection and replication by enhancing viral incorporation of innate anti-HIV-1 protein A3G: a non-pathogenic Nef mutant-based anti-HIV strategy.

Linden A Green, Ying Liu, Johnny J He

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.3field-weighted citation impact, top 22% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 22 citations in OpenAlex.

  1. Pooled it
  2. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

Linden A GreenDepartment of Microbiology and Immunology Walther Cancer Institute, Indianapolis, Indiana 46206.
Ying LiuDepartment of Microbiology and Immunology Walther Cancer Institute, Indianapolis, Indiana 46206.
Johnny J HeDepartment of Microbiology and Immunology Walther Cancer Institute, Indianapolis, Indiana 46206; Center for AIDS Research Walther Cancer Institute, Indianapolis, Indiana 46206; Walther Oncology Center, Indiana University School of Medicine and Walther Cancer Institute, Indianapolis, Indiana 46206; Walther Cancer Institute, Indianapolis, Indiana 46206. Electronic address: jjhe@iupui.edu.
Walther Cancer Foundation · USIndiana University – Purdue University Indianapolis · US

Funding

MECHANISMS OF HIV-1 ENTRY AND PATHOGENESIS IN ASTROCYTESR01NS039804 · NINDS · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI HE, JOHNNY J · 2000 to 2008
$2.3M
Use a novel Tat transgenic model to develop neuroAIDS therapeuticsR21DA022986 · NIDA · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI HE, JOHNNY J · 2006 to 2007
$391k
Drug Abuse and NeuroAIDS in ChinaR21DA025487 · NIDA · INDIANA UNIVERSITY INDIANAPOLIS · PI HE, JOHNNY J · 2008 to 2008
$140k
NIDA NIH HHS R21DA022986NIDA NIH HHS R21DA025487NINDS NIH HHS R01NS039804
6 · The paper itself

Abstract

APOBEC3G (A3G) is a cellular protein that has been identified as an innate anti-human immunodeficiency virus type 1 (HIV-1) factor. One of the major functions of HIV-1 virion infectivity protein (Vif) protein is to target A3G for ubiquitination/proteasome-mediated degradation and, as a result, evade the host innate defense mechanism. Thus, we wished to devise a strategy to restore the anti-HIV activity of A3G by actively targeting it into HIV-1 virions and countering HIV-1 Vif-targeted degradation. In the current study we performed a series of proof-of-concept experiments for this strategy using as a delivery vehicle of A3G, a derivate of non-pathogenic Nef mutant Nef7 that is capable of being efficiently incorporated into HIV-1 virions. We demonstrate that the Nef7.A3G fusion protein retains several important properties of Nef7; that is, the higher virion incorporation efficiency, no PAK-2 (p21-activated kinase 2) activation, and no CD4 and major histocompatibility complex I down-regulation. Meanwhile, we show that virion incorporated Nef7.A3G possesses the anti-HIV infectivity function of A3G. Moreover, we show that virus-like particle-mediated inverse fusion delivery of Nef7.A3G into HIV-infected CD4+ T lymphocytes leads to potent inhibition of HIV-1 replication in these cells. Taken together, these results indicate that Nef7.A3G can effectively restrict HIV infection and replication by restoring the virion incorporation of A3G, even in the presence of Vif.

Indexed as

MutationAPOBEC-3G DeaminaseCD4-Positive T-LymphocytesCytidine DeaminaseHeLa CellsHIV-1HIV InfectionsHumansnef Gene Products, Human Immunodeficiency Virusp21-Activated KinasesProteasome Endopeptidase ComplexRecombinant Fusion ProteinsUbiquitinationvif Gene Products, Human Immunodeficiency VirusVirionVirus AssemblyAPOBEC-3G DeaminaseAPOBEC3G protein, humanCytidine Deaminasenef Gene Products, Human Immunodeficiency Virusnef protein, Human immunodeficiency virus 1p21-Activated KinasesPAK2 protein, humanProteasome Endopeptidase ComplexRecombinant Fusion Proteinsvif Gene Products, Human Immunodeficiency Virusvif protein, Human immunodeficiency virus 1

Identifiers

PMID19324886
PMCPMC2679436
OpenAlexW1996179550

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.