Evidence map›Paper›PMID 10623724›Full record

ArticleJournal of virology2000

A recombinant human immunodeficiency virus type 1 envelope glycoprotein complex stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits is an antigenic mimic of the trimeric virion-associated structure.

J M Binley, R W Sanders, B Clas, N Schuelke, A Master, Y Guo, F Kajumo, D J Anselma, P J Maddon, W C Olson and 1 more

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 348 papers.

0numbers the graph read from it
0cells of the map it votes in
348citing papers in PubMed
8.7field-weighted citation impact, top 1% 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

348 citing papers in PubMed, 528 citations in OpenAlex.

  1. Trial
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  9. Antibody feedback establishes an affinity brake in the germinal center.bioRxiv : the preprint server for biology · 2025
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  12. Macropinosomes are a site of HIV-1 entry into primary CD4Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Article
  14. Article
  15. Article
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  17. Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like conformation.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Article
  20. Article

288 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

11 authors at 4 institutions in 2 countries.

J M BinleyAaron Diamond AIDS Research Center, The Rockefeller University, New York, New York 10016, USA.
R W Sanders
B Clas
N Schuelke
A Master
Y Guo
F Kajumo
D J Anselma
P J Maddon
W C Olson
J P Moore
Aaron Diamond AIDS Research Center · USProgenics Pharmaceuticals (United States) · USRockefeller University · USUniversity of Amsterdam · NL

Funding

MODIFIED ENVELOPE GLYCOPROTEINS FOR HIV1 VACCINER01AI045463 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 1999 to 2010
$4.2M
TOPOLOGICAL ANALYSIS OF HIV-1 ENVELOPE GLYCOPROTEINSR01AI039420 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1996 to 2004
$1.6M
NIAID NIH HHS R01 AI039420NIAID NIH HHS R01 AI045463NIAID NIH HHS R01 AI 39420NIAID NIH HHS R01 AI 45463
6 · The paper itself

Abstract

The few antibodies that can potently neutralize human immunodeficiency virus type 1 (HIV-1) recognize the limited number of envelope glycoprotein epitopes exposed on infectious virions. These native envelope glycoprotein complexes comprise three gp120 subunits noncovalently and weakly associated with three gp41 moieties. The individual subunits induce neutralizing antibodies inefficiently but raise many nonneutralizing antibodies. Consequently, recombinant envelope glycoproteins do not elicit strong antiviral antibody responses, particularly against primary HIV-1 isolates. To try to develop recombinant proteins that are better antigenic mimics of the native envelope glycoprotein complex, we have introduced a disulfide bond between the C-terminal region of gp120 and the immunodominant segment of the gp41 ectodomain. The resulting gp140 protein is processed efficiently, producing a properly folded envelope glycoprotein complex. The association of gp120 with gp41 is now stabilized by the supplementary intermolecular disulfide bond, which forms with approximately 50% efficiency. The gp140 protein has antigenic properties which resemble those of the virion-associated complex. This type of gp140 protein may be worth evaluating for immunogenicity as a component of a multivalent HIV-1 vaccine.

Indexed as

HIV-1Amino Acid SequenceAmino Acid SubstitutionAntigens, ViralCell Line, TransformedCentrifugation, Density GradientChromatography, GelCysteineDisulfidesenv Gene Products, Human Immunodeficiency VirusFurinGene Products, envGlycoproteinsHIV Envelope Protein gp120HIV Envelope Protein gp41HumansAntigens, ViralCysteineDisulfidesenv Gene Products, Human Immunodeficiency VirusFurinGene Products, envGlycoproteinsgp140 envelope protein, Human immunodeficiency virus 1HIV Envelope Protein gp120HIV Envelope Protein gp41Recombinant Fusion ProteinsSubtilisinsSucrose

Identifiers

PMID10623724
PMCPMC111582
OpenAlexW2129274180

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.