Evidence map›Paper›PMID 7540648›Full record

ArticleThe Journal of experimental medicine1995

Human immunodeficiency virus type 1 neutralization is determined by epitope exposure on the gp120 oligomer.

Q J Sattentau, J P Moore

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of experimental medicine, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 172 papers.

0numbers the graph read from it
0cells of the map it votes in
172citing papers in PubMed
6.3field-weighted citation impact, top 2% 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

172 citing papers in PubMed, 333 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021
    Review
  7. Review
  8. Exploitation of glycosylation in enveloped virus pathobiology.Biochimica et biophysica acta. General subjects · 2019
    Review
  9. Article
  10. Article
  11. Protein and Glycan Mimicry in HIV Vaccine Design.Journal of molecular biology · 2019
    Review
  12. Article
  13. Observational
  14. Article
  15. Neutralization tiers of HIV-1.Current opinion in HIV and AIDS · 2018
    Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Germline-targeting immunogens.Immunological reviews · 2017
    Review

112 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Q J SattentauCentre d'Immunologie de Marseille Luminy, Marseille, France.
J P Moore
Centre d’Immunologie de Marseille-Luminy · FR

Funding

VIROLOGY COREP30AI027742 · NIAID · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ZOLLA-PAZNER, SUSAN B · 1989 to 2010
$19.4M
NEUTRALIZATION OF PRIMARY HIV1 VIRUSESR37AI036082 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 1998 to 2017
$7.0M
Neutralization of Primate Immunodeficiency VirusesR01AI036082 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI JOHN P MOORE · 1994 to 2026
$4.3M
NIAID NIH HHS AI-27742NIAID NIH HHS AI-36082
6 · The paper itself

Abstract

The major target of the neutralizing antibody response to infection by the human immunodeficiency virus type 1 (HIV-1) is the outer envelope glycoprotein, gp120. The spectrum of HIV-1 neutralization specificity is currently represented by monoclonal antibodies (mAbs) that can be divided broadly into five groups. We have studied the binding of these mAbs to functional oligomeric and soluble monomeric gp120 derived from the molecular clone of a cell line-adapted isolate of HIV-1, and compared these binding properties with virus neutralization. Binding of all mAbs except those reactive with the V3 loop was much weaker to oligomeric than to monomeric gp120. This reduction in binding to oligomeric gp120 was determined mostly by a slower relative rate of association, although the dissociation rate also had some influence on relative variation in mAb affinity. Virus neutralization correlated broadly with mAb binding to the oligomeric rather than to the monomeric form of gp120, and neutralization potency was related to the estimated association rate. Thus, with the exception of the hypervariable V3 loop, regions of HIV-1 gp120 with the potential to induce a neutralization response are likely to be poorly presented for antibody recognition on the surface of cell line-adapted virions.

Indexed as

Antibodies, MonoclonalAntibody AffinityAntigen-Antibody ReactionsCD4 AntigensCell LineEpitopesHIV-1HIV AntibodiesHIV Envelope Protein gp120HumansNeutralization TestsPeptide FragmentsVirionAntibodies, MonoclonalCD4 AntigensEpitopesHIV AntibodiesHIV Envelope Protein gp120HIV envelope protein gp120 (305-321)Peptide Fragments

Identifiers

PMID7540648
PMCPMC2192089
OpenAlexW2131906141

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.