Evidence map›Paper›PMID 10799583›Full record

ArticleJournal of virology2000

Variable-loop-deleted variants of the human immunodeficiency virus type 1 envelope glycoprotein can be stabilized by an intermolecular disulfide bond between the gp120 and gp41 subunits.

R W Sanders, L Schiffner, A Master, F Kajumo, Y Guo, T Dragic, J P Moore, J M Binley

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 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

69 citing papers in PubMed, 113 citations in OpenAlex.

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9 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

8 authors at 3 institutions in 2 countries.

R W SandersDepartment of Human Retrovirology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands.
L Schiffner
A Master
F Kajumo
Y Guo
T Dragic
J P Moore
J M Binley
Aaron Diamond AIDS Research Center · USRockefeller University · USAcademic Medical Center · NL

Funding

Pure and Authentic HIV-1 Env ImmunogensR01AI093278 · NIAID · TORREY PINES INST FOR MOLECULAR STUDIES · PI BINLEY, JAMES M · 2011 to 2024
$11.6M
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 AI093278NIAID NIH HHS R01 AI 39420NIAID NIH HHS R01 AI 45463
6 · The paper itself

Abstract

We have described an oligomeric gp140 envelope glycoprotein from human immunodeficiency virus type 1 that is stabilized by an intermolecular disulfide bond between gp120 and the gp41 ectodomain, termed SOS gp140 (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 J. P. Moore, J. Virol. 74:627-643, 2000). In this protein, the protease cleavage site between gp120 and gp41 is fully utilized. Here we report the characterization of gp140 variants that have deletions in the first, second, and/or third variable loop (V1, V2, and V3 loops). The SOS disulfide bond formed efficiently in gp140s containing a single loop deletion or a combination deletion of the V1 and V2 loops. However, deletion of all three variable loops prevented formation of the SOS disulfide bond. Some variable-loop-deleted gp140s were not fully processed to their gp120 and gp41 constituents even when the furin protease was cotransfected. The exposure of the gp120-gp41 cleavage site is probably affected in these proteins, even though the disabling change is in a region of gp120 distal from the cleavage site. Antigenic characterization of the variable-loop-deleted SOS gp140 proteins revealed that deletion of the variable loops uncovers cryptic, conserved neutralization epitopes near the coreceptor-binding site on gp120. These modified, disulfide-stabilized glycoproteins might be useful as immunogens.

Indexed as

Genetic VariationAmino Acid SequenceBinding SitesCD4 AntigensDisulfidesenv Gene Products, Human Immunodeficiency VirusEpitopes, B-LymphocyteGene Products, envHIV-1HIV Envelope Protein gp120HIV Envelope Protein gp41HumansMolecular Sequence DataMutagenesisProtein Processing, Post-TranslationalCD4 AntigensDisulfidesenv Gene Products, Human Immunodeficiency VirusEpitopes, B-LymphocyteGene Products, envgp140 envelope protein, Human immunodeficiency virus 1HIV Envelope Protein gp120HIV Envelope Protein gp41

Identifiers

PMID10799583
PMCPMC110861
OpenAlexW2125066176

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.