Evidence map›Paper›PMID 16282475›Full record

ArticleJournal of virology2005

Single-molecule analysis of human immunodeficiency virus type 1 gp120-receptor interactions in living cells.

Melissa I Chang, Porntula Panorchan, Terrence M Dobrowsky, Yiider Tseng, Denis Wirtz

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

35 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Molecular Mechanism of HIV-1 Entry.Trends in microbiology · 2019
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Influenza virus binds its host cell using multiple dynamic interactions.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  17. Review
  18. Article
  19. Review
  20. AFM force measurements of the gp120-sCD4 and gp120 or CD4 antigen-antibody interactions.Biochemical and biophysical research communications · 2011
    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

5 authors at 1 institution in 1 country.

Melissa I ChangDepartment of Chemical and Biomolecular Engineering, The Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA.
Porntula Panorchan
Terrence M Dobrowsky
Yiider Tseng
Denis Wirtz
Johns Hopkins University · US

Funding

Temporal and Spatial Control of the Cell Cycle in Caulobacter CrescentusR01GM065835 · NIGMS · YALE UNIVERSITY · PI JACOBS-WAGNER, CHRISTINE · 2003 to 2016
$3.7M
NIGMS NIH HHS R01 GM065835
6 · The paper itself

Abstract

A quantitative description of the binding interactions between human immunodeficiency virus (HIV) type 1 envelope glycoproteins and their host cell surface receptors remains incomplete. Here, we introduce a single-molecule analysis that directly probes the binding interactions between an individual viral subunit gp120 and a single receptor CD4 and/or chemokine coreceptor CCR5 in living cells. This analysis differentiates single-molecule binding from multimolecule avidity and shows that, while the presence of CD4 is required for gp120 binding to CCR5, the force required to rupture a single gp120-coreceptor bond is significantly higher and its lifetime is much longer than those of a single gp120-receptor bond. The lifetimes of these bonds are themselves shorter than those of the P-selectin/PSGL-1 bond involved in leukocyte attachment to the endothelium bonds during an inflammation response. These results suggest an amended model of HIV entry in which, immediately after the association of gp120 to its receptor, gp120 seeks its coreceptor to rapidly form a new bond. This "bond transfer" occurs only if CCR5 is in close proximity to CD4 and CD4 is still attached to gp120. The analysis presented here may serve as a general framework to study mechanisms of receptor-mediated interactions between viral envelope proteins and host cell receptors at the single-molecule level in living cells.

Indexed as

CD4 AntigensCell LineHIV-1HIV Envelope Protein gp120HumansReceptors, CCR5Receptors, CytokineReceptors, HIVCD4 AntigensHIV Envelope Protein gp120Receptors, CCR5Receptors, CytokineReceptors, HIV

Identifiers

PMID16282475
PMCPMC1287567
OpenAlexW2117555836

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.