Evidence map›Paper›PMID 17144914›Full record

ArticleRetrovirology2006

Kinetic studies of HIV-1 and HIV-2 envelope glycoprotein-mediated fusion.

Stephen A Gallo, Jacqueline D Reeves, Himanshu Garg, Brian Foley, Robert W Doms, Robert Blumenthal

Open access · goldAbstract read
In one paragraph

Article in Retrovirology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

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  18. Peptides modulating conformational changes in secreted chaperones: from in silico design to preclinical proof of concept.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  19. Integrin alphavbeta1 promotes infection by human metapneumovirus.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  20. Review
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 5 institutions in 1 country.

Stephen A GalloCenter for Cancer Research Nanobiology Program, National Cancer Institute at Frederick, National Institutes of Health, Frederick, MD, USA. sgallo@aibs.org
Jacqueline D Reeves
Himanshu Garg
Brian Foley
Robert W Doms
Robert Blumenthal
University of Pennsylvania · USCenter for Cancer Research · USFrederick National Laboratory for Cancer Research · USLos Alamos National Laboratory · USNational Institutes of Health · US

Funding

Intramural NIH HHSNIMHD NIH HHS L60 MD003100
6 · The paper itself

Abstract

backgroundHIV envelope glycoprotein (Env)-mediated fusion is driven by the concerted coalescence of the HIV gp41 N-helical and C-helical regions, which results in the formation of 6 helix bundles. Kinetics of HIV Env-mediated fusion is an important determinant of sensitivity to entry inhibitors and antibodies. However, the parameters that govern the HIV Env fusion cascade have yet to be fully elucidated. We address this issue by comparing the kinetics HIV-1IIIB Env with those mediated by HIV-2 from two strains with different affinities for CD4 and CXCR4.

resultsHIV-1 and HIV-2 Env-mediated cell fusion occurred with half times of about 60 and 30 min, respectively. Binding experiments of soluble HIV gp120 proteins to CD4 and co-receptor did not correlate with the differences in kinetics of fusion mediated by the three different HIV Envs. However, escape from inhibition by reagents that block gp120-CD4 binding, CD4-induced CXCR4 binding and 6-helix bundle formation, respectively, indicated large difference between HIV-1 and HIV-2 envelope glycoproteins in their CD4-induced rates of engagement with CXCR4.

conclusionThe HIV-2 Env proteins studied here exhibited a significantly reduced window of time between the engagement of gp120 with CD4 and exposure of the CXCR4 binding site on gp120 as compared with HIV-1IIIB Env. The efficiency with which HIV-2 Env undergoes this CD4-induced conformational change is the major cause of the relatively rapid rate of HIV-2 Env mediated-fusion.

Indexed as

Membrane FusionCD4 AntigensCell LineHeLa CellsHIV-1HIV-2HIV Envelope Protein gp120HIV Fusion InhibitorsHumansKineticsReceptors, CXCR4CD4 AntigensHIV Envelope Protein gp120HIV Fusion InhibitorsReceptors, CXCR4

Identifiers

PMID17144914
PMCPMC1693918
OpenAlexW2161702294

What OpenQuestion holds

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LicenceCC BY
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.