Evidence map›Paper›PMID 18480458›Full record

ArticleJournal of virology2008

Monitoring early fusion dynamics of human immunodeficiency virus type 1 at single-molecule resolution.

Terrence M Dobrowsky, Yan Zhou, Sean X Sun, Robert F Siliciano, Denis Wirtz

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

25 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Molecular Mechanism of HIV-1 Entry.Trends in microbiology · 2019
    Review
  10. Article
  11. A method for tethering single viral particles for virus-cell interaction studies with optical tweezers.Proceedings of SPIE--the International Society for Optical Engineering · 2018
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Review
  19. 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
  20. 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 2 institutions in 1 country.

Terrence M DobrowskyDepartment of Chemical and Biomolecular Engineering, Johns Hopkins University, 3400 N. Charles St., Baltimore, MD 21218, USA.
Yan Zhou
Sean X Sun
Robert F Siliciano
Denis Wirtz
Johns Hopkins University · USHoward Hughes Medical Institute · US

Funding

Bacterial Division and the Dynamics of the Z-ringR01GM075305 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SUN, SEAN X · 2005 to 2014
$2.9M
Magnetic quantum dots for active sensing of the nuclear envelopeR21EB006890 · NIBIB · JOHNS HOPKINS UNIVERSITY · PI WIRTZ, DENIS · 2007 to 2008
$443k
Howard Hughes Medical InstituteNIBIB NIH HHS EB006890-02NIBIB NIH HHS R21 EB006890NIGMS NIH HHS GM075305-01NIGMS NIH HHS R01 GM075305
6 · The paper itself

Abstract

The fusion of human immunodeficiency virus type 1 (HIV-1) to host cells is a dynamic process governed by the interaction between glycoproteins on the viral envelope and the major receptor, CD4, and coreceptor on the surface of the cell. How these receptors organize at the virion-cell interface to promote a fusion-competent site is not well understood. Using single-molecule force spectroscopy, we map the tensile strengths, lifetimes, and energy barriers of individual intermolecular bonds between CCR5-tropic HIV-1 gp120 and its receptors CD4 and CCR5 or CXCR4 as a function of the interaction time with the cell. According to the Bell model, at short times of contact between cell and virion, the gp120-CD4 bond is able to withstand forces up to 35 pN and has an initial lifetime of 0.27 s and an intermolecular length of interaction of 0.34 nm. The initial bond also has an energy barrier of 6.7 k(B)T (where k(B) is Boltzmann's constant and T is absolute temperature). However, within 0.3 s, individual gp120-CD4 bonds undergo rapid destabilization accompanied by a shortened lifetime and a lowered tensile strength. This destabilization is significantly enhanced by the coreceptor CCR5, not by CXCR4 or fusion inhibitors, which suggests that it is directly related to a conformational change in the gp120-CD4 bond. These measurements highlight the instability and low tensile strength of gp120-receptor bonds, uncover a synergistic role for CCR5 in the progression of the gp120-CD4 bond, and suggest that the cell-virus adhesion complex is functionally arranged about a long-lived gp120-coreceptor bond.

Indexed as

Virus AttachmentVirus InternalizationCD4 AntigensHIV-1HIV Envelope Protein gp120HumansKineticsProtein BindingReceptors, CCR5Receptors, CXCR4Spectrum AnalysisCD4 AntigensCXCR4 protein, humangp120 protein, Human immunodeficiency virus 1HIV Envelope Protein gp120Receptors, CCR5Receptors, CXCR4

Identifiers

PMID18480458
PMCPMC2446967
OpenAlexW2151475382

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.