Evidence map›Paper›PMID 19815247›Full record

ArticleVirology2009

Effect of trimerization motifs on quaternary structure, antigenicity, and immunogenicity of a noncleavable HIV-1 gp140 envelope glycoprotein.

Sean X Du, Rebecca J Idiart, Ellaine B Mariano, Helen Chen, Peifeng Jiang, Li Xu, Kristin M Ostrow, Terri Wrin, Pham Phung, James M Binley and 3 more

Abstract read
In one paragraph

Article in Virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design.International journal of molecular sciences · 2021
    Review
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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

13 authors at 3 institutions in 1 country.

Sean X DuMaxygen, Inc., 515 Galveston Drive, Redwood City, CA 94063, USA.
Rebecca J Idiart
Ellaine B Mariano
Helen Chen
Peifeng Jiang
Li Xu
Kristin M Ostrow
Terri Wrin
Pham Phung
James M Binley
Christos J Petropoulos
John A Ballantyne
Robert G Whalen
Maxygen (United States) · USTorrey Pines Institute For Molecular Studies · USAldevron (United States) · US

Funding

Viral Neutralization AssaysP01AI056375 · NIAID · MAXYGEN, INC. · PI WHALEN, ROBERT G. · 2005 to 2009
$11.1M
SELECTING ENV TRIMERS IN HIV-VLP VACCINE PRESENTATIONSR01AI058763 · NIAID · TORREY PINES INST FOR MOLECULAR STUDIES · PI BINLEY, JAMES M · 2004 to 2007
$1.9M
Selecting Env Trimers in HIV-VLP Vaccine PresentationsR56AI058763 · NIAID · TORREY PINES INST FOR MOLECULAR STUDIES · PI BINLEY, JAMES M · 2008 to 2009
$591k
Creation of Stable Cleaved Trimers of the HIV-1 Envelope ProteinR43AI070032 · NIAID · MAXYGEN, INC. · PI WHALEN, ROBERT GERALD · 2006 to 2006
$240k
NIAID NIH HHS AI 58763NIAID NIH HHS P01 AI 056375NIAID NIH HHS P01 AI056375NIAID NIH HHS R01 AI058763NIAID NIH HHS R43 AI 070032NIAID NIH HHS R43 AI070032NIAID NIH HHS R56 AI058763
6 · The paper itself

Abstract

The external domains of the HIV-1 envelope glycoprotein (gp120 and the gp41 ectodomain, collectively known as gp140) contain all known viral neutralization epitopes. Various strategies have been used to create soluble trimers of the envelope to mimic the structure of the native viral protein, including mutation of the gp120-gp41 cleavage site, introduction of disulfide bonds, and fusion to heterologous trimerization motifs. We compared the effects on quaternary structure, antigenicity, and immunogenicity of three such motifs: T4 fibritin, a GCN4 variant, and the Escherichia coli aspartate transcarbamoylase catalytic subunit. Fusion of each motif to the C-terminus of a noncleavable JRCSF gp140(-) envelope protein led to enhanced trimerization but had limited effects on the antigenic profile and CD4-binding ability of the trimers. Immunization of rabbits provided no evidence that the trimerized gp140(-) constructs induced significantly improved neutralizing antibodies to several HIV-1 pseudoviruses, compared to gp140 lacking a trimerization motif. However, modest differences in both binding specificity and neutralizing antibody responses were observed among the various immunogens.

Indexed as

Protein MultimerizationAmino Acid MotifsAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibody FormationAntigens, ViralCell Lineenv Gene Products, Human Immunodeficiency VirusHIV AntibodiesHumansProtein Structure, QuaternaryRabbitsAntibodies, MonoclonalAntibodies, NeutralizingAntigens, Viralenv Gene Products, Human Immunodeficiency Virusgp140 envelope protein, Human immunodeficiency virus 1HIV Antibodies

Identifiers

PMID19815247
PMCPMC2801758
OpenAlexW2092620639

What OpenQuestion holds

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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.