Evidence map›Paper›PMID 11932429›Full record

ArticleJournal of virology2002

Highly stable trimers formed by human immunodeficiency virus type 1 envelope glycoproteins fused with the trimeric motif of T4 bacteriophage fibritin.

Xinzhen Yang, Juliette Lee, Erin M Mahony, Peter D Kwong, Richard Wyatt, Joseph Sodroski

Abstract read
In one paragraph

Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.

0numbers the graph read from it
0cells of the map it votes in
159citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

159 citing papers in PubMed, 276 citations in OpenAlex.

  1. Review
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  7. Unveiling the invisible genomic dynamics.Experimental & molecular medicine · 2025
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  19. Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design.International journal of molecular sciences · 2021
    Review

99 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

6 authors at 4 institutions in 2 countries.

Xinzhen YangDepartment of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
Juliette Lee
Erin M Mahony
Peter D Kwong
Richard Wyatt
Joseph Sodroski
Dana-Farber Cancer Institute · USHarvard University · USInstitute of Structural and Molecular Biology · GBNational Institute of Allergy and Infectious Diseases · US

Funding

HIV-1 ENVELOPE GLYCOPROTEINSR37AI024755 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1996 to 2015
$11.6M
DFCI-BIDMC-CH CENTER FOR AIDS RESEARCHP30AI028691 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1989 to 2003
$6.2M
MOLECULAR STUDIES OF HIV1 NEUTRALIZING ANTIBODIESR01AI031783 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1991 to 2007
$2.9M
TOPOLOGICAL ANALYSIS OF HIV-1 ENVELOPE GLYCOPROTEINSR01AI039420 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1996 to 2004
$1.6M
Design Of ImmunogensZ01AI005024 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI KWONG, PETER D · 2002 to 2008
$564k
ROLE OF THE HTLV-III ENVELOPE GLYCOPROTEIN IN VIRUSR01AI024755 · NIAID · DANA-FARBER CANCER INSTITUTE · PI SODROSKI, JOSEPH G · 1987 to 1995
–
NIAID NIH HHS AI24755NIAID NIH HHS AI28691NIAID NIH HHS AI31783NIAID NIH HHS AI39420NIAID NIH HHS P30 AI028691NIAID NIH HHS R01 AI031783NIAID NIH HHS R01 AI039420NIAID NIH HHS R37 AI024755
6 · The paper itself

Abstract

The envelope glycoproteins of human immunodeficiency virus type 1 (HIV-1) function as a trimer composed of three gp120 exterior glycoproteins and three gp41 transmembrane proteins. Soluble gp140 glycoproteins composed of the uncleaved ectodomains of gp120 and gp41 form unstable, heterogeneous oligomers, but soluble gp140 trimers can be stabilized by fusion with a C-terminal, trimeric GCN4 motif (X. Yang et al., J. Virol. 74:5716-5725, 2000). To understand the influence of the C-terminal trimerization domain on the properties of soluble HIV-1 envelope glycoprotein trimers, uncleaved, soluble gp140 glycoproteins were stabilized by fusion with another trimeric motif derived from T4 bacteriophage fibritin. The fibritin construct was more stable to heat and reducing conditions than the GCN4 construct. Both GCN4- and fibritin-stabilized soluble gp140 glycoproteins exhibited patterns of neutralizing and nonneutralizing antibody binding expected for the functional envelope glycoprotein spike. Of note, two potently neutralizing antibodies, immunoglobulin G1b12 and 2G12, exhibited the greatest recognition of the stabilized, soluble trimers, relative to recognition of the gp120 monomer. The observed similarities between the GCN4 and fibritin constructs indicate that the HIV-1 envelope glycoprotein ectodomains dictate many of the antigenic and structural features of these fusion proteins. The melting temperatures and ligand recognition properties of the GCN4- and fibritin-stabilized soluble gp140 glycoproteins suggest that these molecules assume conformations distinct from that of the fusion-active, six-helix bundle.

Indexed as

Antibodies, MonoclonalCD4 AntigensHIV-1HIV Envelope Protein gp120HIV Envelope Protein gp41HumansProtein ConformationReceptors, CCR5Recombinant Fusion ProteinsViral ProteinsAntibodies, MonoclonalCD4 Antigensfibritin protein, Enterobacteria phage T4HIV Envelope Protein gp120HIV Envelope Protein gp41Receptors, CCR5Recombinant Fusion ProteinsViral Proteins

Identifiers

PMID11932429
PMCPMC155086
OpenAlexW2105841559

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.