Evidence map›Paper›PMID 14747548›Full record

ArticleJournal of virology2004

Chimeric human immunodeficiency virus type 1 (HIV-1) virions containing HIV-2 or simian immunodeficiency virus Nef are resistant to cyclosporine treatment.

Mahfuz Khan, Lingling Jin, Ming Bo Huang, Lesa Miles, Vincent C Bond, Michael D Powell

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.3field-weighted citation impact, top 50% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure of cyclophilin from Leishmania donovani at 1.97 A resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2007
    Article
  4. Article
  5. Article
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

6 authors at 1 institution in 1 country.

Mahfuz KhanDepartment of Microbiology, Biochemistry, and Immunology, Morehouse School of Medicine, Atlanta, Georgia 30310, USA.
Lingling Jin
Ming Bo Huang
Lesa Miles
Vincent C Bond
Michael D Powell
Morehouse School of Medicine · US

Funding

Morehouse School of Medicine Center of Excellence Research Endowment ProgramS21MD000101 · NIMHD · MOREHOUSE SCHOOL OF MEDICINE · PI MONTGOMERY-RICE, VALERIE C. · 2001 to 2015
$74.3M
TRANSCRIPTION FACTORS AND PROSTATE CANCERG12RR003034 · NCRR · MOREHOUSE SCHOOL OF MEDICINE · PI ZHAO, XUEYING · 1986 to 2011
$32.4M
Vascular Cell Apoptosis: Mediator Role of Transforming Growth Factor-beta-1S06GM008248 · NIGMS · MOREHOUSE SCHOOL OF MEDICINE · PI YANG, QINGLIN · 1989 to 2009
$19.8M
NCRR NIH HHS G12 RR003034NCRR NIH HHS G12-RR03034NIGMS NIH HHS S06 GM008248NIGMS NIH HHS S06GM08248NIMHD NIH HHS S21 MD000101
6 · The paper itself

Abstract

The viral protein Nef and the cellular factor cyclophilin A are both required for full infectivity of human immunodeficiency virus type 1 (HIV-1) virions. In contrast, HIV-2 and simian immunodeficiency virus (SIV) do not incorporate cyclophilin A into virions or need it for full infectivity. Since Nef and cyclophilin A appear to act in similar ways on postentry events, we determined whether chimeric HIV-1 virions that contained either HIV-2 or SIV Nef would have a direct effect on cyclophilin A dependence. Our results show that chimeric HIV-1 virions containing either HIV-2 or SIV Nef are resistant to treatment by cyclosporine and enhance the infectivity of virions with mutations in the cyclophilin A binding loop of Gag. Amino acids at the C terminus of HIV-2 and SIV are necessary for inducing cyclosporine resistance. However, transferring these amino acids to the C terminus of HIV-1 Nef is insufficient to induce cyclosporine resistance in HIV-1. These results suggest that HIV-2 and SIV Nef are able to compensate for the need for cyclophilin A for full infectivity and that amino acids present at the C termini of these proteins are important for this function.

Indexed as

Drug Resistance, ViralRecombination, GeneticAmino Acid SequenceCyclophilin ACyclosporineGene Products, nefHeLa CellsHIV-1HIV-2HumansMolecular Sequence Datanef Gene Products, Human Immunodeficiency VirusViral Regulatory and Accessory ProteinsVirionCyclophilin ACyclosporineGene Products, nefnef Gene Products, Human Immunodeficiency VirusNEF protein, SIVViral Regulatory and Accessory Proteins

Identifiers

PMID14747548
PMCPMC369439
OpenAlexW2109931473

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.